Method and compositions for determining enzymatic activity and specificity of methyltransferases

ABSTRACT

The invention provides crystalline O-methyltransferases and isolated non-native O-methyltransferases as well as sets of their structural coordinates. Also provided are methods of predicting the activity or substrate specificity of putative O-methyltransferases, methods of identifying potential substrates of O-methyltransferases, and methods of identifying potential inhibitors of methyltransferases.

FIELD OF THE INVENTION

The present invention relates to methods for designing O-methyltransferases, and to predicting the activity and/or substrate specificity of native and mutated O-methyltransferases. The present invention further relates to methods for identifying O-methyltransferase substrates and/or inhibitors.

BACKGROUND

Advances in molecular biology have allowed the development of biological agents useful in modulating protein activity or nucleic acid expression, respectively. Many of these advances are based on the knowledge of the primary sequence of the molecule to be modulated. For example, the knowledge of the nucleic acid sequence of DNA or RNA allows the development of antisense or ribozyme molecules. Similarly, the knowledge of the primary sequence allows for the identification of sequences that may be useful in creating monoclonal antibodies. Often, however, the knowledge of the primary sequence of a protein is insufficient to allow development of therapeutic or diagnostic molecules due to the secondary, tertiary or quartenary structure of the protein from which the primary sequence is obtained. In addition, mere knowledge of the primary sequence of a protein is insufficient to allow development of novel enzymes that facilitate the production of novel products or production of known reaction products under desired conditions (i.e., conditions under which such conversion does not ordinarily occur). The process of designing potent and specific inhibitors, activators, or novel proteins has improved with the arrival of techniques for determining the three-dimensional structure of an enzyme or polypeptide, whose activity substrate specificity or resulting enzymatic product one desires to modulate.

Methylation of oxygen (O-methylation), nitrogen (N-methylation), and carbon (C-methylation) is a universal process critical to all organisms. In plants, the O-methylation patterns of polyhydroxylated small molecules are of particular utility and importance. These site-specific reactions are crucial to determining final product distribution via multiple branched biosynthetic pathways using the same or similar intermediates and substrates. For example, the secondary metabolic pathway of phenylpropanoid biosynthesis utilizes cinnamate and acetate units to construct a diverse set of hydroxylated and polycyclic aromatic compounds which are used for regulatory, structural, and functional purposes in plants including protection against UV photodamage, pigmentation, fertilization, signaling, gene induction, anti-microbial defense, chemoattraction, and structural support. Additionally, phytochemicals mediate important biological activities in mammals. For example, isoflavones such as formononetin, (7-hydroxy-4′-methoxyisoflavone), daidzein (4′,7-dihydroxyisoflavone), and genistein (4′,5,7-trihydroxyisoflavone) possess phytoestrogenic and anti-oxidant activity. Consumption of a diet high in flavonoid and isoflavonoid compounds is salutary in reducing the incidence of certain types of cancer and lowering the risk for cardiovascular disease. Site specific methylation of flavonoid and isoflavonoid derivatives modulates their in vivo activity by limiting the number of reactive hydroxyl groups, altering the solubility properties of the resulting products, and ultimately determining whether a particular small molecule will interact with cellular receptors.

O-methylation is a common downstream modification. Although several 5-adenosyl-L-methionine (SAM)-dependent O-methyltransferase (OMT) genes have been found in polyketide synthase (PKS) gene clusters (Decker, H. et al. J. Bacteriol. (1993) 175:3876-3886), their specificities have not been systematically studied as yet. It is suspected that some of them could be useful for combinatorial biosynthesis. For instance, O-11-methylation occurs in several members of the anthracycline, tetracenomycin, and angucycline classes of aromatic polyketides.

An improvement in the understanding of the structure/function of these enzymes would allow for a number of advances in the art, e.g., the exploitation of the synthetic capabilities of known enzymes for production of useful new chemical compounds, for the creation of novel non-native enzymes having new synthetic capabilities and the like. The present invention addresses this and related needs.

SUMMARY OF THE INVENTION

The present invention provides crystalline O-methyltransferases and isolated non-native O-methyltransferases having a set of structural coordinates of said crystalline O-methyltransferases. Also disclosed are methods of predicting the activity and/or substrate specificity of a putative O-methyltransferases, methods of identifying potential O-methyltransferases substrates, and methods of identifying potential O-methyltransferases inhibitors.

Other aspects, embodiments, advantages, and features of the present invention will become apparent from the following specification.

BRIEF DESCRIPTION OF FIGURES

FIG. 1 shows a phenylpropanoid biosynthetic pathway in Medicago sativa L (alfalfa). Carbon flow begins in primary metabolism by making use of phenylalanine, which ultimately serves as the building block for a diverse class of plant secondary metabolites. The enzymes depicted are PAL (phenylalanine-ammonia lyase), CA4H (cinnamic acid 4-hydroxylase), 4CL (4-coumarate:coenzyme A ligase), CHS (chalcone synthase), CHR (chalcone reductase), ChOMT (2′,4,4′-trihydroxychalcone 2′-hydroxyl-O-methyltransferase), CHI (chalcone isomerase), IFS (isoflavone synthase), IOMT (isoflavone-O-methyltransferase or isoflavanone-O-methyltransferase), IFOH (isoflavone 2′-hydroxylase), IFR (isoflavone reductase), and PTS (pterocarpan synthase). Also depicted are the reaction substrates and products S-adenosyl-L-methionine (SAM) as a methyl source, yielding S-adenosyl-L-homocysteine (SAH). (The reaction depicted in the solid black box occurs in vitro and likely represents a cryptic activity of IOMT, which would be expected to methylate an isoflavanone intermediate. The depicted dehydration step can spontaneously occur in solution over time or is catalyzed by a specific dehydratase enzyme. A-rings are derived from the head-to-tail condensation of malonyl-CoA derived acetyl groups and the B-rings are derived from the p-coumaryl moiety.

FIG. 2 collectively shows the architecture of ChOMT and IOMT monomers.

FIG. 2A shows a stereo view of the ChOMT monomer's Cα backbone. Every 20 Cα atoms are numbered and the N-terminus and C-terminus are labeled. The disordered loop between residues 160 and 173 is shown as a dashed coil.

FIG. 2B shows a stereo view of the final SIGMAA-weighted 2|Fo−Fc| electron density map of the ChOMT active site encompassing bound SAH and isoliquiritigenin molecules. Putative hydrogen bonds are shown as dashed cylinders. Single letter amino acid codes are used: The map is contoured at 1.5σ.

FIG. 2C shows a stereo view of the IOMT monomer's Cα backbone. Every 20 Cα atoms are numbered and the N-terminus and C-terminus are labeled.

FIG. 2D shows a stereo view of the final SIGMAA-weighted 2|Fo−Fc| electron density map of the IOMT active site encompassing bound SAH and isoformononetin molecules. Putative hydrogen bonds are shown as dashed cylinders. Single letter amino acid codes are used. The map is contoured at 1.5σ.

FIG. 3 collectively shows the architecture of a ChOMT dimer and active site.

FIG. 3A shows a ribbon and molecular surface representation of a ChOMT homodimer. Monomer A and monomer B are shown, and bound SAH and isoliquiritigenin molecules are indicated by the arrows.

FIG. 3B shows a close-up stereo view of the substrate binding site highlighting some of the hydrogen bonding and van der Waals interactions with SAH. The view is shown in the same orientation as in FIG. 3A.

FIG. 3C shows a close-up stereo view of the substrate binding site highlighting some of the hydrogen bonding and van der Waals interactions with a bound isoliquiritigenin. Residues labeled with (B) designate side chains residing on the symmetric monomer. Ribbon diagrams are produced with MOLSCRIPT and the surface is produced with GRASP. Both are rendered with POV-ray. Some side chains have been omitted for clarity.

FIG. 4 collectively shows the architecture of an IOMT dimer and active site.

FIG. 4A shows a ribbon and molecular surface representation of the IOMT homodimer. Monomer A and monomer B are shown, and bound SAH and isoformononetin molecules are indicated by arrows.

FIG. 4B shows a close-up stereo view of the substrate binding site highlighting some of the hydrogen bonding and van der Waals interactions with SAH. The view is shown in the same orientation as in FIG. 4A.

FIG. 4C shows a close-up stereo view of the substrate binding site highlighting some of the hydrogen bonding and van der Waals interactions with the bound product, isoformononetin. Residues labeled with (B) designate side chains residing on the symmetric monomer. Some side chains have been omitted for clarity.

FIG. 5 collectively shows structural and sequence comparisons of representative OMTs.

FIG. 5A shows a structural comparison of isoflavone O-methyltransferase (IOMT), HhaI DNA C-methyltransferase (M.HhaI), and catechol O-methyltransferase (COMT). SAH, isoformononetin (IOMT), SAM (M.HhaI), SAM, and dinitrocatechol (COMT) are rendered as stick models. The conserved SAM/SAH binding domains and the non-conserved regions are shown. The reactions catalyzed by IOMT, and “COMT” are illustrated with the transferred methyl group highlighted in light shading. “COMT” differs from the plant OMT, COMT, which stands for caffeic acid O-methyltransferase.

FIG. 5B shows a sequence alignment of nine representative plant O-methyltransferases (SEQ ID NOS: 1-9). Primary and secondary structure of IOMT from Medicago sativa (alfalfa; AAC49927) and ChOMT from Medicago sativa (alfalfa; AAB48059) are presented in FIG. 5B as well as sequence alignment of caffeic acid OMT from Medicago sativa (alfalfa; AAB46623), scoulerine OMT from Coptis japonica (goldenthread; BAA06192), isoeugenol OMT from Clarkia breweri (fairy fans; AAC01533), hydroxymaakiain OMT from Pisum sativa (pea; AAC49856), diphenol OMT from Capsicum annum (hot pepper; AAC17455), catechol OMT from Nicotiana tabacum (tobacco; CAA52461), and flavonoid OMT from Hordeum vulgare (barley; CAA54616). α-Helices are indicated by cylinders and β-strands as arrows. The numbering of each protein is in parentheses with every tenth position dotted. Residues involved in SAM/SAH binding (dark shading), substrate binding (underlined), substrate binding in trans from the dyad related polypeptide (boxed), and catalysis (light shading) are highlighted.

FIG. 6 collectively shows the ChOMT and IOMT active sites.

FIG. 6A shows a ChOMT-isoliquiritigenin complex. The ribbon diagram approximates the global orientation of the ChOMT dimer used for the close-up view of the complete chalcone binding site depicted in stereo. The black box highlights the region of ChOMT shown in stereo. Bonds are coded by atom type with isoliquiritigenin carbon atoms in dark shading and protein carbon atoms in light shading. Hydrogen bonds are depicted as dashed cylinders and water molecules as spheres. Residues labeled with (B) are contributed by the symmetric polypeptide chain.

FIG. 6B shows an IOMT-isoformononetin complex (top panel) and a model of a putative IOMT-(2S,3S)-2,4′,7-trihydroxyisoflavanone complex (bottom panel) generated by the superposition of the B-ring of isoformononetin and the A-ring of 2,4′,7-trihydroxyisoflavanone. The ribbon diagram approximates the global orientation of the IOMT dimer used for the close-up view of the isoflavone binding site depicted in stereo. The black box highlights the region of IOMT shown in stereo. Bonds are coded by atom type with isoflavone and isoflavanone carbon atoms in dark shading and protein carbon atoms in light shading. Hydrogen bonds are depicted as dashed cylinders.

FIG. 7 collectively shows an autoradiograph of ChOMT and IOMT catalytic histidine mutants.

FIG. 7A lanes 1 to 6 refer to ChOMT wild type, H278L, H278A, H278Q, H278K, and H278N, respectively. ¹⁴C-methylated 4,4′-dihydroxy-2′-methoxychalcone is labeled.

FIG. 7B lanes 1 to 6 correspond to IOMT wild type, H257L, H257I, H257Q, H257K, and H257D, respectively. ¹⁴C-methylated product 4′-hydroxy-7-methoxyisoflavone (isoformononetin) is labeled.

FIG. 8 shows an example of a computer system in block diagram form.

DETAILED DESCRIPTION OF THE INVENTION

Plant small molecule O-methyltransferases utilize S-adenosyl-L-methionine (SAM) as a methyl source, yielding S-adenosyl-L-homocysteine (SAH) and methyl ether derivatives of plant small molecules as products. This family of enzymes must conserve the ability to bind SAM binding while affording a sufficient degree of active site diversity to bind and correctly position a variety of disparate small molecules. Substrate discrimination by these plant O-methyltransferases (OMTs) is considerable given that plants synthesize several thousand phenylpropanoid compounds often with multiple hydroxyl groups. While certain plant methyltransferases, such as caffeic acid O-methyltransferase (COMT), demonstrate greater substrate promiscuity by methylating caffeoyl and 5-hydroxy coniferyl alcohols, aldehydes, and free acids, the core scaffolds of these substrates are conserved, with the differences occurring at the propanoid tail of the molecules. The activity profiles of COMT against these substrates show a high degree of variability, suggesting a kinetic preference for substrates in vivo. The majority of plant OMTs act on unique substrates and catalyze O-methylations at specific sites with little or no activity towards other constituent hydroxyl moieties or towards related compounds.

Chalcone O-methyltransferase (ChOMT) is a small molecule methyltransferase found in Medicago sativa L (alfalfa). ChOMT methylates the 2′-hydroxyl of isoliquiritigenin (2′,4,4′-trihydroxychalcone), converting it to 4,4′-dihydroxy-2′-methoxychalcone, a potent nodulation (nod) gene inducer of soil rhizobia. Among the diverse compounds released from alfalfa roots, 4,4′-dihydroxy-2′-methoxychalcone acts as the most efficient transcriptional activator of nod genes, activating nodABC through interaction with the transcriptional regulators nodD1 and nodD2 of Rhizobium meliloti. Additionally, ChOMT is an important branch point enzyme in phenylpropanoid biosynthesis in alfalfa. Methylation of isoliquiritigenin prevents the chalcone isomerase (CHI) catalyzed cyclization of isoliquiritigenin to the flavanone liquiritigenin (7,4′-dihydroxyflavanone). Once cyclized, flavanones serve as starting materials for the biosynthesis of a variety of structurally diverse natural products including anthocyanins, flavones, flavonols, isoflavones, and pterocarpans. Many of these compounds serve as important UV protectants, pigments, anti-microbial phytoalexins in leguminous plants, and the like (FIG. 1).

Isoflavone O-methyltransferase (IOMT) is essential for the biosynthesis of medicarpin, the major phytoalexin of alfalfa. In vivo studies demonstrate that IOMT is necessary for the formation of formononetin (7-hydroxy-4′-methoxyisoflavone). In vitro assays using daidzein (4′,7-dihydroxyisoflavone) as a substrate and in vivo studies conducted in the absence of fungal elicitation of IOMT overexpressing plants yield the compound isoformononetin (4′-hydroxy-7-methoxyisoflavone). This compound is rarely found in plants and has no known biological role in plant physiology. However, when elicited with CuCl₂ or infection with Phoma medicaginis, IOMT overexpressing plants accumulate the 4′-O-methylated isoflavonoid formononetin and the downstream phytoalexin derived from it, medicarpin (FIG. 1). In the unperturbed medicarpin biosynthetic pathway, IOMT almost certainly never encounters daidzein thus producing no isoformononetin in vivo. While IOMT will methylate daidzein, this compound is not the in vivo substrate of IOMT. The apparent disparate results concerning IOMT methylation of daidzein in vitro to form isoformononetin and the absence of this compound in plants, strongly implicates an unstable intermediate, most likely the product of isoflavone synthase (IFS) as the true in vivo substrate for IOMT. The putative product of the cytochrome P450 enzyme IFS and substrate for IOMT is 2,7,4′-trihydroxyisoflavanone, a reactive intermediate in isoflavone biosynthesis. Because this isoflavanone is unstable in aqueous solution, the full identification and characterization of the IFS product is incomplete. However, over-expression of IOMT in transgenic alfalfa leads to increased production of 4′-O-methylated isoflavonoids. Alfalfa microsomes containing IOMT can convert 4′,7-dihydroxyisoflavanone to the physiological product formononetin, thus implicating the formation of an IFS/IOMT complex during medicarpin biosynthesis.

The present invention provides for the first time the x-ray crystal structure coordinates of ChOMT (Appendix A and C) and IOMT (Appendix B and D), two 5-adenosyl-L-methionine (SAM) dependent OMTs from Medicago sativa L. ChOMT and IOMT are 40 kDa proteins and exist as homodimers in solution. These methyltransferases possess SAM binding domains that align structurally with previously characterized viral, bacterial, archaebacterial, and mammalian OMT's. The fold of the catalytic SAM binding domain is conserved throughout all classes of SAM-dependent methyltransferases. Unique features of this family of plant O-methyltransferases include the presence of a second domain involved in dimerization and the contribution of the dimer interface to the substrate-binding site. The structures presented here complexed with substrates and products reveal a characteristic mechanism for methyl transfer by this family of plant OMTs. Furthermore, these studies provide the first structural understanding of substrate discrimination displayed by this large family of plant OMTs.

As used herein “O-methyltransferase” or “OMT” includes a diverse family of plant O-methyltransferase enzymes that catalyze transfer of a methyl group to various substrates.

Both ChOMT and IOMT were crystallized from polyethylene glycol (PEG) solutions in the presence of a two-fold molar excess of SAM or SAH. The nucleic acid and amino acid sequences of ChOMT and IOMT are shown in Table 1 (SEQ ID NO: 1 and 2) and 2 (SEQ ID NO: 3 and 4), respectively. Structures of ChOMT and IOMT were determined with seleno-methionine (Se-met) substituted proteins using multiwavelength anomalous dispersion (MAD) phasing. Additional structures of substrate and product complexes were determined by molecular replacement based on the Se-met derived structures (FIG. 2A-D).

TABLE 1 ChOMT SEQUENCE Nucleic Acid Sequence aaaaaaaaat cattagttct aatcaaaaaa tgggaaattc ctacattacc aaggaggata accaaattag tgctacctca gaacaaactg aagacagtgc atgtctttca gcaatggtac ttaccactaa tcttgtttat ccagcagtgt taaatgctgc tattgatctc aatttatttg agatcatagc taaggcaaca ccacctggtg ctttcatgtc accatctgaa attgcttcta aattaccagc atcaacgcag cactcggact tgcctaatag gcttgaccgc atgctgcgtt tgcttgctag ttattctgtt cttacttcca ctactcgaac cattgaggat ggtggtgccg agagagttta cggactctca atggtcggaa aataccttgt ccctgatgaa agtagaggtt atttggcttc atttactaca tttctatgtt atcctgcatt attacaagtt tggatgaatt ttaaggaagc ggtggtggat gaagacattg acttgttcaa gaacgttcat ggagtgacaa agtatgaatt catgggaaag gataaaaaaa tgaaccaaat ttttaacaaa tcaatggttg atgtatgtgc tacagagatg aaaagaatgc ttgaaatata cactggattt gagggaatat caacattagt tgatgttgga ggtggaagtg gaagaaatct tgaattgata atatccaaat atccattaat aaagggaatt aactttgatc ttccccaagt tattgaaaat gcaccaccac tttcagggat tgagcatgtt ggaggagata tgtttgcaag tgttccacag ggtgatgcca tgatactgaa ggctgtatgc cataattggt cagatgaaaa atgcatagaa tttttaagca attgtcacaa agctttatca ccaaatggaa aagtgattat tgtggagttc atattgccag aagaaccaaa cacaagtgaa gaatctaagc ttgtttcaac tcttgacaat ctcatgttta tcacagttgg tggaagggaa agaactgaga aacaatatga gaaattgagc aaactctctg gattttccaa atttcaagtt gcttgccgtg ctttcaacag tttgggagtg atggaatttt ataaatgaag taattacaac aataactttg gattttaaga tcaatgtgtt aagagtaaag tgagaaaata aaggcctttt gtgaggtcat gttgttttac aatgtactcg ttataattcc tgctatgatg ttatgtaatg tttatgcaat taagaaaaaa Amino Acid Sequence MGNSYITKEDNQISATSEQTEDSACLSAMVLTTNLVYPAVLNAAIDLNLFEIIAKATPPGAFMSPSEIA SKLPASTQHSDLPNRLDRMLRLLASYSVLTSTTRTIEDGGAERVYGLSMVGKYLVPDESRGYLASFTTF LCYPALLQVWMNFKEAVVDEDIDLFKNVHGVTKYEFMGKDKKMNQIFNKSMVDVCATEMKRMLEIYTGF EGISTLVDVGGGSGRNLELIISKYPLIKGINFDLPQVIENAPPLSGIEHVGGDMFASVPQGDAMILKAV CHNWSDEKCIEFLSNCHKALSPNGKVIIVEFILPEEPNTSEESKLVSTLDNLMFITVGGRERTEKQYEK LSKLSGFSKFQVACRAFNSLGVMEFYK

TABLE 2 IOMT SEQUENCE Nucleic Acid Sequence caaaaattca tttgcaaaaa aaaatggcgt catcaattaa tggcagaaaa ccaagtgaaa ttttcaaagc acaagcttta ttatacaaac acatatatgc cttcatagat tccatgtctc ttaaatgggc tgttggaatg aacataccaa acataatcca caaccatggc aaaccaattt ctctttcaaa cttagtttca attcttcaag ttccatcgtc gaaaataggt aacgtgcggc gtctcatgcg ttaccttgcg cacaacggat tcttcgagat aattacaaaa gaagaagagt cttatgctct cactgttgct tcagagcttc ttgttagagg cagtgatctt tgtttagcac cgatggttga gtgtgttctt gatccaactc tttcgggttc gtatcatgag ctgaagaaat ggatttatga ggaagatctt acactctttg gtgttacttt aggatctggt ttttgggatt ttcttgataa aaatcctgaa tataatacat catttaatga tgcaatggct agtgattcta aattgataaa cttggcattg agagattgtg attttgtgtt tgatggattg gaatcaattg tggatgttgg tggtggaact ggaacaactg ctaagattat ttgtgagact tttcctaagt tgaaatgtat tgtgtttgat aggccacaag ttgtagagaa cttatctgga agcaataatt tgacttatgt tggtggggac atgttcacat ctattcctaa tgctgatgca gttttgctta agtatattct acataattgg actgataagg attgcctaag gatactgaag aaatgtaaag aagctgttac aaatgatggg aaaagaggaa aagtgactat tatagacatg gtgataaatg aaaaaaaaga tgagaatcaa gttactcaaa ttaagctcct tatggatgta aacatggctt gtctaaatgg aaaagagaga aatgaggaag aatggaagaa actcttcata gaagctggtt tccaacacta taagatatct cctttgactg gatttttgtc tcttattgag atctatccat aaacactttt gctttgatca ttcatccatt ctattgtttc atgttataaa ccaatcttgt tctctattat gatatctcac ttgtaatatg catttgttgg tacaaataat agaatttgca tacatgtaaa aaaaaaaaaa aaaaaaa Amino Acid Sequence MASSINGRKPSEIFKAQALLYKHIYAFIDSMSLKWAVGMNIPNIIHNHGKPISLSNLVSILQVPSSKIG NVRRLMRYLAHNGFFEIITKEEESYALTVASELLVRGSDLCLAPMVECVLDPTLSGSYHELKKWIYEED LTLFGVTLGSGFWDFLDKNPEYNTSFNDAMASDSKLINLALRDCDFVFDGLESIVDVGGGTGTTAKIIC ETFPKLKCIVFDRPQVVENLSGSNNLTYVGGDMFTSIPNADAVLLKYILHNWTDKDCLRILKKCKEAVT NDGKRGKVTIIDMVINEKKDENQVTQIKLLMDVNMACLNGKERNEEEWKKLFIEAGFQHYKISPLTGFL SLIEIYP

ChOMT (FIG. 3A-C) and IOMT (FIG. 4A-C) exhibit a common tertiary structure consisting of a large C-terminal catalytic domain responsible for SAM binding and substrate methylation and a smaller N-terminal domain involved in dimerization and formation of the back wall of the substrate binding site. Due to this conservation of fold, the root mean square deviation (RMSD) for alignment of the catalytic domains is 1.4 Å, while both the catalytic and dimerization domains align with an RMSD of 1.8 Å for all backbone atoms. The catalytic domain contains a core α/β Rossmann fold common to nucleotide binding proteins. Structural alignments with representative DNA and small molecule methyltransferases illustrate the presence of a conserved fold involved in SAM/SAH binding (FIG. 5A). Unlike most structurally characterized methyltransferases that are monomeric, ChOMT and IOMT form homologous homodimers in their respective crystalline lattices. The monomers in both cases are related by a crystallographic two-fold axis. While ChOMT and IOMT were originally characterized as monomers, the recombinant proteins exhibit no monomer formation in solution. Dimerization appears to be critical for activity and most likely occurs in vivo as well as in vitro. In fact, the presence of a dimerization interface appears to be common to plant OMT's and intimately contribute to substrate binding.

Plants elegantly modulate the methyltransferase fold, which is conserved throughout all kingdoms, in order to gain remarkable specificity and diversity in substrate recognition. This exquisite selectivity occurs through reconfiguration of the active site surface via side chain variation around the substrate-binding pocket. Added diversity in the active site topology is attained through modulation of the dimerization interface. Many of the amino acids directly involved in substrate binding are sequentially conserved in ChOMT and IOMT. However, the size of these residues varies due to the need to accommodate different but chemically related substrates (FIG. 5B).

Alterations in amino acid composition not only sterically modify the active site, but also provide unique hydrogen-bonding scaffolds that lead to diverse substrate specificities and different distributions of methylated products. Furthermore, the abundance of methionine residues in the active site used to sequester aromatic moieties is an important feature of these plant phenolic natural product methyltransferases. This conserved methionine motif may be a widespread element utilized by plant aromatic OMTs to encapsulate their hydrophobic and aromatic rich substrates. Additionally, the pre-organization of the active site allows for facile substrate acceptance and helps restrict active site promiscuity by selecting for a unique small molecule scaffold. Upon SAM binding, the active site appears pre-arranged for substrate binding as evidenced by the low RMSD values of 0.4 Å for the structures with and without substrate/product bound.

Because methylation patterns in large part determine product outcome, subtle alterations in methyltransferase substrate selectivity have a profound impact on secondary metabolic activities in plant cells. The high-resolution crystal structures in complex with substrates and products described herein provide the first three dimensional picture of a diverse family of plant natural product biosynthetic enzymes and serve as a structural foundation for understanding the stereochemical principles underlying plant O-methyltransferase activity and substrate selectivity.

Due to the common structural characteristics of ChOMT and IOMT as well as related characteristics (e.g., the conserved fold involved in SAM/SAH binding), the crystal structures and atomic coordinates provided by the present invention have applicability to a family of plant O-methyltransferase enzymes including, for example, caffeic acid OMT from Medicago sativa (alfalfa; AAB46623), scoulerine OMT from Coptis japonica (goldenthread; BAA06192), isoeugenol OMT from Clarkia breweri (fairy fans; AAC01533), hydroxymaakiain OMT from Pisum sativa (pea; AAC49856), diphenol OMT from Capsicum annum (hot pepper; AAC17455), catechol OMT from Nicotiana tabacum (tobacco; CAA52461), and flavonoid OMT from Hordeum vulgare (barley; CAA54616).

Based both upon the structures of ChOMT and IOMT and sequence alignments with the large family of plant OMTs (see, e.g., FIG. 5B), methylation most likely proceeds via base-assisted deprotonation of the hydroxyl group followed by a nucleophilic attack of the newly generated phenolate anion of the substrate on the reactive methyl group of SAM. In ChOMT, deprotonation of the 2′-hydroxyl group of the A-ring by His 278, sets up the subsequent attack by the resulting hydroxyl anion on the methyl group of SAM. Because the sulfur of SAM is positively charged, the transmethylation process is facilitated by the deprotonation step. Glu 306 and Glu 337 bracket the catalytic histidine, with a hydrogen-bonding interaction of the Nδ nitrogen to the carboxylate group of Glu 337 (FIG. 2B). This interaction ensures the optimal orientation of the imidazole group for deprotonation of the T-hydroxyl of the isoliquiritigenin substrate by the Nδ-nitrogen of His 278 (FIG. 6A). Mutations of His 278 to leucine, alanine, glutamine, lysine, and asparagine completely eliminated methyltransferase activity further implicating His 278 as an important catalytic residue (FIG. 7A).

Catalysis by IOMT proceeds through a comparable mechanism with His 257 serving as the base responsible for deprotonation of the 7-hydroxyl group on the A-ring of daidzein (FIG. 6B). Similarly to ChOMT, Asp 288 and Glu 318 sterically constrain His 257 and position the Nδ-nitrogen through a hydrogen bond with Glu 318. This same catalytic mechanism would be predicted for the putative physiological to substrate, 2,7,4′-trihydroxyisoflavanone. Mutations of His 257 to leucine, isoleucine, glutamine, and aspartate eliminated methyltransferase activity towards daidzein. Mutation of the active site histidine to lysine displayed greatly diminished activity compared to wild type enzyme (FIG. 7B).

Other methyltransferases follow similar bimolecular nucleophilic substitution reaction (SN₂) pathways involving oxygen, nitrogen, and carbon based nucleophiles. The addition of methyl groups to carbon, such as seen in the C5 methylation of cytosine, usually proceeds via initial attack of an active site cysteine on C6, generating a resonance-stabilized carbanion at C5. Small molecule O-methylation reactions, such as in catechol O-methyltransferase, are facilitated by metal-mediated deprotonation. Glycine N-methyltransferase and PvuII DNA-(cytosine N4) methyltransferase are postulated to use a glutamate residue to deprotonate the amino moiety thus facilitating methyl transfer. The putative role of histidine as a catalytic base has only been seen in one other structurally characterized methyltransferase, PRMT3 (protein arginine N-methyltransferase). The reaction mechanism by which histidine functions as a catalytic base in ChOMT and IOMT is similar to the reaction mechanism proposed for PRMT3, which utilizes a His-Asp proton relay system.

In ChOMT, the extensive dimerization interface buries approximately 8990 Å² of surface area, encompassing 30% of the available surface area of the dimer (FIG. 3A). Met 29, Thr 32, and Thr 33 insert into the catalytic domain of the neighboring molecule thus forming the back wall of the neighboring molecule's active site. The extent of the IOMT interface is comparable with 8597 Å² of buried surface area at the interface, comprising approximately 30% of the available surface area of the dim (FIG. 4A). Tyr 25, Phe 27, and Ile 28 form the back wall of the catalytic domain of the dyad related monomer.

“Active Site” refers to a site in a ChOMT or IOMT defined by amino acid residues that interact with substrate and facilitate a biosynthetic reaction that allows one or more products to be produced. An active site is comprised of α-carbon atoms to that are indirectly linked via peptide bonds. The position in three-dimensional space of an α-carbon at the active site of a ChOMT and IOMT and of R-groups associated therewith can be determined using techniques such as three-dimensional modeling based upon the structural coordinates provided by the present invention or by X-ray crystallography, and/or techniques associated therewith.

Accordingly, for the first time, the invention provides the ability to modulate activity of the active site of O-methyltransferases (e.g., ChOMT and IOMT) to design novel enzymes to catalyze the synthesis of various hydroxylated and methoxylated compounds, which are used for regulatory, structural, and functional purposes, including, for example, protection against UV photodamage, pigmentation, fertilization, signaling, gene induction, anti-microbial defense, chemoattraction, structural support, and the like. The present invention allows the comparison of the activities of various O-methyltransferases and designed mutants of O-methyltransferases by computer modeling as well as by biological assays.

The three-dimensional structure of ChOMT and IOMT, provided herein, together with the structure of Chalcone Synthase and Chalcone Isomerase (see PCT/US00/20674, filed Jul. 27, 2000, entitled, “METHODS AND COMPOSITIONS FOR DETERMINING ENZYMATIC ACTIVITY”; and PCT/US01/27027, filed Aug. 29, 2001, entitled, “METHODS AND COMPOSITIONS FOR DETERMINING ISOMERASE ENZYMATIC ACTIVITY”) (both of which are incorporated by reference herein), provides a useful template for engineering experiments that aim to diversify and modify phenylpropanoid biosynthetic pathways for crop and food sources, as well as providing novel phenylpropanoid for intermediates and leads in drug discovery.

As used herein, “naturally occurring amino acid” and “naturally occurring R-group” includes L-isomers of the twenty amino acids naturally occurring in proteins. Naturally occurring amino acids are glycine, alanine, valine, leucine, isoleucine, serine, methionine, threonine, phenylalanine, tyrosine, tryptophan, cysteine, proline, histidine, aspartic acid, asparagine, glutamic acid, glutamine, arginine, and lysine. Unless specially indicated, all amino acids referred to in this application are in the L-form.

“Unnatural amino acid” and “unnatural R-group” includes amino acids that are not naturally found in proteins. Examples of unnatural amino acids included herein are racemic mixtures of selenocysteine and selenomethionine. In addition, unnatural amino acids include the D or L forms of, for example, nor-leucine, para-nitrophenylalanine, homophenylalanine, para-fluorophenylalanine, 3-amino-2-benzylpropionic acid, homoarginines, D-phenylalanine, and the like.

“R-group” refers to the substituent attached to the α-carbon of an amino acid residue. An R-group is an important determinant of the overall chemical character of an amino acid. There are twenty natural R-groups found in proteins, which make up the twenty naturally occurring amino acids.

“α-carbon” refers to the chiral carbon atom found in an amino acid residue. Typically, four substituents will be covalently bound to said α-carbon including an amine group, a carboxylic acid group, a hydrogen atom, and an R-group.

“Positively charged amino acid” and “positively charged R-group” includes any naturally occurring or unnatural amino acid having a positively charged side chain under normal physiological conditions. Examples of positively charged, naturally occurring amino acids include arginine, lysine, histidine, and the like.

“Negatively charged amino acid” and “negatively charged R-group” includes any naturally occurring or unnatural amino acid having a negatively charged side chain under normal physiological conditions. Examples of negatively charged, naturally occurring amino acids include aspartic acid, glutamic acid, and the like.

“Hydrophobic amino acid” and “hydrophobic R-group” includes any naturally occurring or unnatural amino acid having an uncharged, nonpolar side chain that is relatively insoluble in water. Examples of naturally occurring hydrophobic amino acids are alanine, leucine, isoleucine, valine, proline, phenylalanine, tryptophan, methionine, and the like.

“Hydrophilic amino acid” and “hydrophilic R-group” includes any naturally occurring or unnatural amino acid that is relatively soluble in water. Examples of naturally occurring hydrophilic amino acids include serine, threonine, tyrosine, asparagine, glutamine, cysteine, and the like.

“Mutant” refers to a ChOMT or IOMT enzyme having one or more R-group modifications to the amino acids of a wild-type ChOMT or IOMT or having a substitution of one or more amino acids (either conservative or non-conservative substitutions), that result in a modification to the catalytic activity of a wild-type ChOMT or IOMT. For example, a mutant ChOMT or IOMT has an R-group on one or more α-carbons other than the prescribed arrangements of R-groups associated with one or more α-carbons of a known isolated ChOMT or IOMT. Typically mutants refer to changes or modification to the configuration of R-groups within the active site, however mutations outside of the residues found in the active site are also considered to be mutants in accordance with the present invention.

Non-mutated ChOMT and IOMT includes a ChOMT or IOMT wherein no R-group(s) are changed relative to the active site (see, for example, PDB Accession No. 1FPQ, 1FP1, 1FPX, 1FP2, Appendix A and Appendix B). A nonmutated ChOMT or IOMT according to the present invention may or may not have amino acid residues outside of the active site that are the same as those taught for native ChOMT or IOMT.

The R-groups of known isolated O-methyltransferases can be readily determined by consulting sequence databases well known in the art such as, for example, GenBank, and comparing the sequence of ChOMT or IOMT with the to identified sequence in the database. Additional R-groups found inside and/or outside of the active site may or may not be the same. R-groups may be a natural R-group, unnatural R-group, hydrophobic R-group, hydrophilic R-group, positively charged R-group, negatively charged R-group, and the like.

A “non-native” O-methyltransferase (e.g., ChOMT or IOMT) refers to an O-methyltransferase protein that is not found in nature, whether isolated or not. A non-native O-methyltransferase may, for example, be a mutated O-methyltransferase (including a mutated ChOMT or IOMT).

A “native” O-methyltransferase (e.g., ChOMT or IOMT) refers to O-methyltransferase proteins that are produced in nature, e.g., are not mutated (e.g., a ChOMT having a sequence as set forth in Table 1 (SEQ ID NO: 1 and 2) or an IOMT having a sequence as set forth in Table 2 (SEQ ID NO: 3 and 4)).

“Purified” or “isolated” refers to a protein or nucleic acid, respectively, that has been separated from its natural environment. Contaminant components of its natural environment may include enzymes, hormones, and other proteinaceous or non-proteinaceous solutes. In one embodiment, the isolated molecule, in the case of a protein, will be purified to a degree sufficient to obtain at least 15 residues of N-terminal or internal amino acid sequence or to homogeneity by SDS-PAGE under reducing or non-reducing conditions using Coomassie blue or silver stain. In the case of a nucleic acid the isolated molecule will preferably be purified to a degree sufficient to obtain a nucleic acid sequence using standard sequencing methods.

By a “substantially pure polypeptide” is meant an O-methyltransferase polypeptide (e.g., a ChOMT or IOMT polypeptide) which has been separated from components that naturally accompany it. Typically, the polypeptide is substantially pure when it is at least 60%, by weight, free from the proteins and naturally occurring organic molecules with which it is naturally associated. Preferably, the preparation is at least 75%, more preferably at least 90%, and most preferably at least 99%, by weight, O-methyltransferase polypeptide. A substantially pure O-methyltransferase polypeptide may be obtained, for example, by extraction from a natural source; by expression of a recombinant nucleic acid encoding an O-methyltransferase polypeptide; by chemically synthesizing the protein; and the like. Purity can be measured by any appropriate method (e.g., column chromatography, polyacrylamide gel electrophoresis, by HPLC analysis, and the like).

“Degenerate variations thereof” refers to changing a gene sequence using the degenerate nature of the genetic code to encode proteins having the same amino acid sequence yet having a different gene sequence. For example, an O-methyltransferase of the present invention (e.g., ChOMT or IOMT) is based on amino acid sequences. Degenerate gene variations thereof can be made encoding the same protein due to the plasticity of the genetic code, as described herein.

“Expression” refers to transcription of a gene or nucleic acid sequence, stable accumulation of nucleic acid, and the translation of that nucleic acid to a polypeptide sequence. Expression of genes also involves transcription of the gene to make RNA, processing of RNA into mRNA in eukaryotic systems, and translation of mRNA into proteins. It is not necessary for the genes to integrate into the genome of a cell in order to achieve expression. This definition in no way limits expression to a particular system or to being confined to cells or a particular cell type and is meant to include cellular, transient, in vitro, in vivo, and viral expression systems in both prokaryotic, eukaryotic cells, and the like.

“Foreign” or “heterologous” genes refers to a gene encoding a protein whose exact amino acid sequence is not normally found in the host cell.

“Promoter” and “promoter regulatory element”, and the like, refer to a nucleotide sequence within a nucleic acid fragment or gene that controls the expression of that gene. These can also include expression control sequences. Promoter regulatory elements, and the like, from a variety of sources can be used efficiently to promote gene expression. Promoter regulatory elements are meant to include constitutive, tissue-specific, developmental-specific, inducible, subgenomic promoters, and the like. Promoter regulatory elements may also include certain enhancer elements or silencing elements that improve or regulate transcriptional efficiency. Promoter regulatory elements are recognized by RNA polymerases, promote the binding thereof, and facilitate RNA transcription.

Appendix A lists the atomic structure coordinates for ChOMT as derived by X-ray diffraction from a crystal of a ChOMT complexed with SAH. The following abbreviations are used in Appendix A: “Atom Type” refers to the element whose coordinates are measured. “X, Y, Z” crystallographically define the atomic position of the element measured; and “B” is a thermal factor that measures movement of the atom around its atomic center.

Appendix B lists the atomic structure coordinates for IOMT as derived by X-ray diffraction from a crystal of an IOMT complexed with SAH. The following abbreviations are used in Appendix B: “Atom Type” refers to the element whose coordinates are measured. “X, Y, Z” crystallographically define the atomic position of the element measured; and “B” is a thermal factor that measures movement of the atom around its atomic center.

Appendix C lists the atomic structure coordinates for ChOMT as derived by X-ray diffraction from a crystal of a ChOMT complexed with SAH and isoliquiritigenin. The following abbreviations are used in Appendix B: “Atom Type” refers to the element whose coordinates are measured. “X, Y, Z” crystallographically define the atomic position of the element measured; and “B” is a thermal factor that measures movement of the atom around its atomic center.

Appendix D lists the atomic structure coordinates for IOMT as derived by X-ray diffraction from a crystal of an IOMT complexed with SAH and isoformononetin. The following abbreviations are used in Appendix D: “Atom Type” refers to the element whose coordinates are measured. “X, Y, Z” crystallographically define the atomic position of the element measured; and “B” is a thermal factor that measures movement of the atom around its atomic center.

“Structure coordinates” refers to Cartesian coordinates (x, y, and z positions) derived from mathematical equations involving Fourier synthesis as determined from patterns obtained via diffraction of a monochromatic beam of X-rays by the atoms (scattering centers) of an O-methyltransferase polypeptide in crystal form. Diffraction data are used to calculate electron density maps of repeating protein units in the crystal (unit cell). Electron density maps are used to establish the positions of individual atoms within a crystal's unit cell. The term “crystal structure coordinates” refers to mathematical coordinates derived from mathematical equations related to the patterns obtained on diffraction of a monochromatic beam of X-rays by the atoms (scattering centers) of an O-methyltransferase polypeptide (e.g., a ChOMT or IOMT protein molecule) in crystal form. The diffraction data are used to calculate an electron density map of the repeating unit of the crystal. The electron density maps are used to establish the positions of the individual atoms within the unit cell of the crystal. The crystal structure coordinates of an O-methyltransferase can be obtained from a ChOMT or IOMT protein. Crystals for both proteins grew in space group C2 with one molecule per asymmetric unit. Unit cell dimensions for ChOMT were a=127.19 Å, b=53.79 Å, c=73.55 Å, β=125.55°. IOMT cell dimensions were a=145.56 Å, b=50.54 Å, c=63.82 Å, β=106.69°. The coordinates of the O-methyltransferasepolypeptide can also be obtained by means of computational analysis.

The term “selenomethionine substitution” refers to the method of producing a chemically modified form of the crystal of an O-methyltransferase (e.g., a ChOMT or IOMT). The O-methyltransferase protein is expressed by bacteria in media that is depleted in methionine and supplemented with selenomethionine. Selenium is thereby incorporated into the crystal in place of methionine sulfurs. The location(s) of selenium are determined by X-ray diffraction analysis of the crystal. This information is used to generate the phase information used to construct a three-dimensional structure of the protein.

“Heavy atom derivatization” refers to a method of producing a chemically modified form of an O-methyltransferase crystal. In practice, a crystal is soaked in a solution containing heavy atom salts or organometallic compounds, e.g., lead chloride, gold thiomalate, thimerosal, uranyl acetate, and the like, which can diffuse through the crystal and bind to the protein's surface. Locations of the bound heavy atoms can be determined by X-ray diffraction analysis of the soaked crystal. This information is then used to construct phase information which can then be used to construct three-dimensional structures of the enzyme as described in Blundel, T. L., and Johnson, N. L., Protein Crystallography, Academic Press (1976), which is incorporated herein by reference.

“Unit cell” refers to a basic parallelepiped shaped block. Regular assembly of such blocks may construct the entire volume of a crystal. Each unit cell comprises a complete representation of the unit pattern, the repetition of which builds up the crystal.

“Space Group” refers to the arrangement of symmetry elements within a crystal.

“Molecular replacement” refers to a process for generating a preliminary model of an O-methyltransferase whose structural coordinates are unknown. This is accomplished by orienting and positioning a molecule whose structural coordinates are known within the unit cell of the unknown crystal so as best to account for the observed diffraction pattern of the unknown crystal. Phases can then be calculated from this model and combined with the observed amplitudes to give an approximate Fourier synthesis of the structure whose coordinates are unknown. This in turn can be subject to any of several forms of refinement to provide a final, accurate structure of the unknown crystal (Lattman, E., 1985, in Methods in Enzymology, 11 5.55-77; Rossmann, M G., ed., “The Molecular Replacement Method” 1972, Int. Sci. Rev. Ser., No. 13, Gordon & Breach, New York). Using structure coordinates of the ChOMT or IOMT provided herein, molecular replacement may be used to determine the structural coordinates of a crystalline mutant, homologue, or a different crystal form of an O-methyltransferase.

“Substrate” refers to any compound acted on by the O-methyltransferases (e.g., ChOMT or IOMT) of the invention, mutants thereof disclosed herein, and the like. Examples include trihydroxychalcone, daidzein, and 2,7,4′ trihydroxyisoflavanone, for ChOMT and IOMT, respectively, as well as S-adenosyl-L-methionine (SAM).

“Altered substrate specificity” refers to a change in the ability of a mutant O-methyltransferase to produce an enzymatic product as compared to a non-mutated O-methyltransferase. Altered substrate specificity may include the ability of an O-methyltransferase to exhibit different enzymatic parameters relative to a non-mutated O-methyltransferase (K_(m), V_(max), etc.), use different substrates, and/or produce products that are different from those of known non-native O-methyltransferases.

A polypeptide is a chain of amino acids, regardless of length or post-translational modification (e.g., glycosylation or phosphorylation). A polypeptide or protein refers to a polymer in which the monomers are amino acid residues, which are joined together through amide bonds. When the amino acids are alpha-amino acids, either the L-optical isomer or the D-optical isomer can be used, the L-isomers being typical. A ChOMT polypeptide of the invention is intended to encompass an amino acid sequence as set forth in Table 1 and includes a sequence having one or more mutations, mutants, variants and conservative substitutions thereof comprising L- or D-amino acids and include modified sequences such as glycoproteins. An IOMT polypeptide of the invention is intended to encompass an amino acid sequence as set forth in Table 2 and includes a sequence having one or more mutations, mutants, variants and conservative substitutions thereof comprising L- or D-amino acids and include modified sequences such as glycoproteins.

Accordingly, the polypeptides contemplated for use in the practice of the invention are intended to cover naturally occurring proteins, as well as those that are recombinantly or synthetically synthesized. Polypeptide or protein fragments are also encompassed by the invention. Fragments can have the same or substantially the same amino acid sequence as the naturally occurring protein. A polypeptide or peptide having substantially the same sequence means that an amino acid sequence is largely, but not entirely, the same, but retains a functional activity of the sequence to which it is related. In general polypeptides of the invention include peptides, or full-length proteins, that contain substitutions, deletions, or insertions into the protein backbone, that would still have an approximately 70%-90% homology to the original protein over the corresponding portion. A yet greater degree of departure from homology is allowed if like-amino acids, i.e. conservative amino acid substitutions, do not count as a change in the sequence.

A polypeptide may be substantially related but for a conservative variation, such polypeptides being encompassed by the invention. A conservative variation denotes the replacement of an amino acid residue by another, biologically similar residue. Examples of conservative variations include the substitution of one hydrophobic residue such as isoleucine, valine, leucine or methionine for another, or the substitution of one polar residue for another, such as the substitution of arginine for lysine, glutamic for aspartic acids, or glutamine for asparagine, and the like. Other illustrative examples of conservative substitutions include the changes of: alanine to serine; arginine to lysine; asparagine to glutamine or histidine; aspartate to glutamate; cysteine to serine; glutamine to asparagine; glutamate to aspartate; glycine to proline; histidine to asparagine or glutamine; isoleucine to leucine or valine; leucine to valine or isoleucine; lysine to arginine, glutamine, or glutamate; methionine to leucine or isoleucine; phenylalanine to tyrosine, leucine or methionine; serine to threonine; threonine to serine; tryptophan to tyrosine; tyrosine to tryptophan or phenylalanine; valine to isoleucine or leucine, and the like. The term “conservative variation” also includes the use of a substituted amino acid in place of an unsubstituted parent amino acid provided that antibodies raised to the substituted polypeptide also immunoreact with the unsubstituted polypeptide.

Modifications and substitutions are not limited to replacement of amino acids. For a variety of purposes, such as increased stability, solubility, or configuration concerns, one skilled in the art will recognize the need to introduce (by deletion, replacement, or addition) other modifications. Examples of such other modifications include incorporation of rare amino acids, dextra-amino acids, glycosylation sites, and cytosine for specific disulfide bridge formation. The modified peptides can be chemically synthesized, or the isolated gene can be subjected to site-directed mutagenesis, or a synthetic gene can be synthesized and expressed in bacteria, yeast, baculovirus, tissue culture and so on.

Polypeptides contemplated for use in the practice of the present invention include O-methyltransferase polypeptides (e.g., ChOMT and IOMT) from any number of plants, prokaryotes, eukaryotes, including, for example, invertebrates, mammals and humans and include sequences as set forth in Table 1 (SEQ ID NO: 2) and Table 2 (SEQ ID NO: 4), as well as sequences that have at least 70% homology to the sequence of SEQ ID NO: 2 and 4, fragments, variants, or conservative substitutions of any of the foregoing sequences.

The term “variant” refers to polypeptides that are modified at one or more amino acid residues yet still retain the biological activity of an O-methyltransferase polypeptide. Variants can be produced by any number of means known in the art, including, for example, methods such as, for example, error-prone PCR, shuffling, oligonucleotide-directed mutagenesis, assembly PCR, sexual PCR mutagenesis, and the like, as well as any combination thereof.

By “substantially identical” is meant a polypeptide or nucleic acid exhibiting at least 50%, preferably 85%, more preferably 90%, and most preferably 95% identity to a reference amino acid or nucleic acid sequence. An example of a reference amino acid or nucleic acid sequence can be the sequences set forth in Tables 1 (SEQ ID NO: 1) and Table 2 (SEQ ID NO: 3).

Homology and identity are often measured using sequence analysis software (e.g., Sequence Analysis Software Package of the Genetics Computer Group, University of Wisconsin Biotechnology Center, 1710 University Avenue, Madison, Wis. 53705). Such software matches similar sequences by assigning degrees of homology to various deletions, substitutions and other modifications. The terms “homology” and “identity” in the context of two or more nucleic acids or polypeptide sequences, refer to two or more sequences or subsequences that are the same or have a specified percentage of amino acid residues or nucleotides that are the same when compared and aligned for maximum correspondence over a comparison window or designated region as measured using any number of sequence comparison algorithms or by manual alignment and visual inspection.

For sequence comparison, typically one sequence acts as a reference sequence, to which test sequences are compared. When using a sequence comparison algorithm, test and reference sequences are entered into a computer, subsequence coordinates are designated, if necessary, and sequence algorithm program parameters are designated. Default program parameters can be used, or alternative parameters can be designated. The sequence comparison algorithm then calculates the percent sequence identities for the test sequences relative to the reference sequence, based on the program parameters.

A “comparison window”, as used herein, includes reference to a segment of any one of the number of contiguous positions selected from the group consisting of from 20 to 600, usually about 50 to about 200, more usually about 100 to about 150 in which a sequence may be compared to a reference sequence of the same number of contiguous positions after the two sequences are optimally aligned. Methods of alignment of sequence for comparison are well known in the art. Optimal alignment of sequences for comparison can be conducted, e.g., by the local homology algorithm of Smith & Waterman, Adv. Appl. Math. 2:482, 1981, by the homology alignment algorithm of Needleman & Wunsch, J. Mol. Biol. 48:443, 1970, by the search for similarity method of Person & Lipman, Proc. Nat'l Acad. Sci. USA 85:2444, 1988, by computerized implementations of these algorithms (GAP, BESTFIT, FASTA, and TFASTA in the Wisconsin Genetics Software Package, Genetics Computer Group, 575 Science Dr., Madison, Wis.), or by manual alignment and visual inspection. Other algorithms for determining homology or identity include, for example, in addition to a BLAST program (Basic Local Alignment Search Tool at the National Center for Biological Information), ALIGN, AMAS (Analysis of Multiply Aligned Sequences), AMPS (Protein Multiple Sequence Alignment), ASSET (Aligned Segment Statistical Evaluation Tool), BANDS, BESTSCOR, BIOSCAN (Biological Sequence Comparative Analysis Node), BLIMPS (BLocks IMProved Searcher), FASTA, Intervals & Points, BMB, CLUSTAL V, CLUSTAL W, CONSENSUS, LCONSENSUS, WCONSENSUS, Smith-Waterman algorithm, DARWIN, Las Vegas algorithm, FNAT (Forced Nucleotide Alignment Tool), Framealign, Framesearch, DYNAMIC, FSAP (Fristensky Sequence Analysis Package), GAP (Global Alignment Program), GENAL, GIBBS, GenQuest, ISSC (Sensitive Sequence Comparison), LALIGN (Local Sequence Alignment), LCP (Local Content Program), MACAW (Multiple Alignment Construction & Analysis Workbench), MAP (Multiple Alignment Program), MBLKP, MBLKN, PIMA (Pattern-Induced Multi-sequence Alignment), SAGA (Sequence Alignment by Genetic Algorithm) and WHAT-IF. Such alignment programs can also be used to screen genome databases to identify polynucleotide sequences having substantially identical sequences. A number of genome databases are available, for example, a substantial portion of the human genome is available as part of the Human Genome Sequencing Project (J. Roach, http://weber.u.Washington.edu/˜roach/human_genome_progress2.html) (Gibbs, 1995). At least twenty-one other genomes have already been sequenced, including, for example, M. genitalium (Fraser et al., 1995), M. jannaschii (Bult et al., 1996), H. influenzae (Fleischmann et al., 1995), E. coli (Blattner et al., 1997), and yeast (S. cerevisiae) (Mewes et al., 1997), and D. melanogaster (Adams et al., 2000), mouse, C. elegans, and Arabadopsis sp. Several databases containing genomic information annotated with some functional information are maintained by different organizations, and are accessible via the internet, for example, http://wwwtigr.org/tdb; http://www.genetics.wisc.edu; http://genome-www.stanford.edu/˜ball; http://hiv-web.lanl.gov; http://www.ncbi.nlm.nih.gov; http://www.ebi.ac.uk; http://Pasteur.fr/other/biology; and http://www.genome.wi.mit.edu.

One example of a useful algorithm is BLAST and BLAST 2.0 algorithms, which are described in Altschul et al., Nucl. Acids Res. 25:3389-3402, 1977, and Altschul et al., J. Mol. Biol. 215:403-410, 1990, respectively. Software for performing BLAST analyses is publicly available through the National Center for Biotechnology Information (http://www.ncbi.nlm.nih.gov). This algorithm involves first identifying high scoring sequence pairs (HSPs) by identifying short words of length W in the query sequence, which either match or satisfy some positive-valued threshold score T when aligned with a word of the same length in a database sequence. T is referred to as the neighborhood word score threshold (Altschul et al., supra). These initial neighborhood word hits act as seeds for initiating searches to find longer HSPs containing them. The word hits are extended in both directions along each sequence for as far as the cumulative alignment score can be increased. Cumulative scores are calculated using, for nucleotide sequences, the parameter M (reward score for a pair of matching residues; always >0). For amino acid sequences, a scoring matrix is used to calculate the cumulative score. Extension of the word hits in each direction are halted when: the cumulative alignment score falls off by the quantity X from its maximum achieved value; the cumulative score goes to zero or below, due to the accumulation of one or more negative-scoring residue alignments; or the end of either sequence is reached. The BLAST algorithm parameters W, T, and X determine the sensitivity and speed of the alignment. The BLASTN program (for nucleotide sequences) uses as defaults a wordlength (W) of 11, an expectation (E) of 10, M=5, N=−4 and a comparison of both strands. For amino acid sequences, the BLASTP program uses as defaults a wordlength of 3, and expectations (E) of 10, and the BLOSUM62 scoring matrix (see Henikoff & Henikoff, Proc. Natl. Acad. Sci. USA 89:10915, 1989) alignments (B) of 50, expectation (E) of 10, M=5, N=−4, and a comparison of both strands.

The BLAST algorithm also performs a statistical analysis of the similarity between two sequences (see, e.g., Karlin & Altschul, Proc. Natl. Acad. Sci. USA 90:5873, 1993). One measure of similarity provided by BLAST algorithm is the smallest sum probability (P(N)), which provides an indication of the probability by which a match between two nucleotide or amino acid sequences would occur by chance. For example, a nucleic acid is considered similar to a references sequence if the smallest sum probability in a comparison of the test nucleic acid to the reference nucleic acid is less than about 0.2, more preferably less than about 0.01, and most preferably less than about 0.001.

In one embodiment, protein and nucleic acid sequence homologies are evaluated using the Basic Local Alignment Search Tool (“BLAST”) In particular, five specific BLAST programs are used to perform the following task:

-   -   (1) BLASTP and BLAST3 compare an amino acid query sequence         against a protein sequence database;     -   (2) BLASTN compares a nucleotide query sequence against a         nucleotide sequence database;     -   (3) BLASTX compares the six-frame conceptual translation         products of a query nucleotide sequence (both strands) against a         protein sequence database;     -   (4) TBLASTN compares a query protein sequence against a         nucleotide sequence database translated in all six reading         frames (both strands); and     -   (5) TBLASTX compares the six-frame translations of a nucleotide         query sequence against the six-frame translations of a         nucleotide sequence database.

The BLAST programs identify homologous sequences by identifying similar segments, which are referred to herein as “high-scoring segment pairs,” between a query amino or nucleic acid sequence and a test sequence which is preferably obtained from a protein or nucleic acid sequence database. High-scoring segment pairs are preferably identified (i.e., aligned) by means of a scoring matrix, many of which are known in the art. Preferably, the scoring matrix used is the BLOSUM62 matrix (Gonnet et al., Science 256:1443-1445, 1992; Henikoff and Henikoff, Proteins 17:49-61, 1993). Less preferably, the PAM or PAM250 matrices may also be used (see, e.g., Schwartz and Dayhoff, eds., 1978, Matrices for Detecting Distance Relationships: Atlas of Protein Sequence and Structure, Washington: National Biomedical Research Foundation). BLAST programs are accessible through the U.S. National Library of Medicine, e.g., at www.ncbi.nlm.nih.gov.

The parameters used with the above algorithms may be adapted depending on the sequence length and degree of homology studied. In some embodiments, the parameters may be the default parameters used by the algorithms in the absence of instructions from the user.

One aspect of the invention resides in the prediction of the three-dimensional structure of O-methyltransferases that have amino acid sequences substantially identical (using any of the foregoing techniques and algorithms) to a ChOMT or IOMT sequence set forth in Tables 1 (SEQ ID NO: 2) and Table 2 (SEQ ID NO: 4). O-methyltransferases having substantial identity to a ChOMT or IOMT described herein will have a predicted three dimensional structure as described in Tables 3 or 4 (below) and have coordinates as set forth in Appendix A or B. Using the predicted three-dimensional structure, further modifications to the O-methyltransferase can be made using standard molecular biology techniques (e.g., site directed mutagenesis, and the like). Alternatively, substrates, or inhibitors of the O-methyltransferase can be designed based upon its predicted three-dimensional structure.

Another aspect of the invention resides in obtaining crystals of an O-methyltransferase polypeptide (e.g., ChOMT or IOMT) of sufficient quality to determine the three dimensional (tertiary) structure of the protein by X-ray diffraction methods. The knowledge obtained concerning the three-dimensional structure of such O-methyltransferase can be used in the determination of the three dimensional structure of other O-methyltransferase polypeptides in various metabolic pathways of plants and other organisms (e.g., flavonoid pathway). The structural coordinates of ChOMT and IOMT as set forth herein can be used to develop new O-methyltransferase enzymes or O-methyltransferase binding agents (e.g., inhibitors or substrates) using various computer models. Based on the structural coordinates of the ChOMT and IOMT polypeptide (e.g., the three dimensional protein structure of such polypeptides), as described herein, novel O-methyltransferases can be engineered and identified based on the models and coordinates provided herein. In addition, small molecules, which mimic or are capable of interacting with a functional domain of an O-methyltransferase polypeptide, can be designed and synthesized to modulate plant metabolic pathways, phenylpropanoid synthesis, ChOMT and IOMT activity and other methyltransferase biological functions as well as the biological functions of other phenylpropanoid-related enzymes. Accordingly, in one embodiment, the invention provides a method of “rational” enzyme or drug design.

Another approach to “rational” enzyme or drug design is based on a lead compound that is discovered using high throughput screens; the lead compound is further modified based on a crystal structure of the binding regions of the molecule in question. Accordingly, another aspect of the invention is to provide related protein sequences or material which is a starting material in the rational design of new O-methyltransferases or drugs, which lead to the synthesis of new phenylpropanoid or modify the phenylpropanoid pathway.

The present invention relates to crystallized O-methyltransferases and mutants thereof, from which the position of specific alpha-carbon atoms and R-groups associated therewith comprising the active site can be determined in three-dimensional space. The invention also relates to structural coordinates of ChOMTs and IOMTs, use of said structural coordinates to develop structural information related to ChOMT and IOMT homologues (members of the O-methyltransferase family), mutants, and the like, and to crystal forms of such O-methyltransferases. Furthermore, the invention, as disclosed herein, provides a method whereby the alpha-carbon structural coordinates specifically determined for atoms comprising the active site of ChOMT or IOMT can be used to develop O-methyltransferases wherein R-groups associated with active site alpha-carbon atoms are different from the R-groups found in native O-methyltransferases, e.g., are mutant O-methyltransferases. In addition, the present invention provides for production of mutant ChOMTs and IOMTs based on the structural information provided herein and for use of the mutant ChOMTs and IOMTs to make a variety of phenylpropanoid or flavanoid compounds using a variety of substrates.

The present invention further provides, for the first time, O-methyltransferase crystal coordinates, as exemplified by ChOMT (Appendix A) and IOMT (Appendix B).

Also provided are coordinates for crystals which are grown in the presence and absence of substrate and product, thus allowing definition of the structural or atomic coordinates associated therewith. The structural coordinates allow determination of the alpha-carbon atoms comprising the active site, R-groups associated therewith, and the interaction of said alpha-carbons and said R-groups with each other. For example, ChOMT was co-crystallized with SAH or SAH and isoliquirigenin as a complex (see Appendix A, C and PDB accession numbers 1FPQ, 1FP1, all of which are incorporated herein by reference in their entirety). Other crystallized complexes include IOMT with SAH or SAH and isoformononetin as a complex (see Appendix B, D and PDB Accession Nos. 1FPX, 1FP2, all of which are incorporated herein by reference in their entirety).

Crystal structures are preferably obtained at a resolution of about 1.56 angstroms to about 3 angstroms for an O-methyltransferase in the presence and in the absence of bound substrate or substrate analog. Those skilled in the art understand that a set of structure coordinates determined by X-ray crystallography is not without standard error. Therefore, for the purpose of this invention, any set of structure coordinates wherein the active site alpha-carbons of an O-methyltransferase (e.g., ChOMT or IOMT) homologue, or mutants thereof, have a root mean square deviation less than ±2.3 angstroms when superimposed using the structural coordinates listed in the Appendices for ChOMT or IOMT, respectively, shall be considered identical.

The active site alpha-carbons of ChOMT and IOMT generally are not all contiguous, i.e., are not adjacent to one another in the primary amino acid sequence of the enzyme due to intervening amino acid residues between various active site alpha-carbons. Nevertheless, it should be appreciated that certain active site alpha-carbons can be adjacent to one another in some instances.

An appropriate combination of R-groups, linked to active site alpha-carbons, can facilitate the formation of one or more desired reaction products. The combination of R-groups selected for use in an O-methyltransferase can be any combination other than the ordered arrangements of R-groups found in known native O-methyltransferases (exemplified by ChOMT and IOMT, herein). Typically, R-groups that are found on active site alpha-carbons are those found in naturally occurring amino acids. In some embodiments, however, R-groups other than those found in naturally occurring amino acids can be used.

The present invention permits the use of molecular design techniques to design, select, and synthesize genes encoding mutant O-methyltransferases and O-methyltransferases that produce different and/or novel phenylpropanoid compounds using various substrates. Mutant proteins of the present invention and nucleic acids encoding the same can be designed by genetic manipulation based on structural information of ChOMT and IOMT provided for the first time herein. For example, one or more R-groups associated with the active site alpha-carbon atoms of ChOMT or IOMT can be changed by altering the nucleotide sequence of the corresponding polynucleotide sequence encoding the ChOMT or IOMT, thus making one or more mutant ChOMTs or IOMTs. Such genetic manipulations can be guided by structural information concerning the R-groups found in the active site alpha-carbons when substrate is bound to the protein upon crystallization (as described in Appendices A-D).

Mutant O-methyltransferase proteins of the present invention may be prepared in a number of ways available to the skilled artisan. For example, the polynucleotide sequence encoding wild-type ChOMT or IOMT (as described in Tables 1 (SEQ ID NO: 1) or Table 2 (SEQ ID NO: 3)) may be mutated at those sites identified herein as corresponding to amino acid residues identified in the active site by means currently available to the artisan skilled in molecular biology techniques. Suitable techniques include oligonucleotide-directed mutagenesis, deletion, chemical mutagenesis, and the like. The protein encoded by the mutant polynucleotide is then produced by expressing the polynucleotide in, for example, a bacterial or plant expression system.

Alternatively, O-methyltransferase mutants may be generated by site specific-replacement of a particular amino acid with an unnaturally occurring amino acid or mimetic. As such, O-methyltransferase mutants may be generated through replacement of an amino acid residue or a particular cysteine or methionine residue with selenocysteine or selenomethionine. This may be achieved by growing a host organism capable of expressing either the wild type or mutant polypeptide on a growth medium depleted of natural cysteine or methionine or both and growing on medium enriched with either selenocysteine, selenomethionine, or both. These and similar techniques are described in Sambrook et al., (Molecular Cloning, A Laboratory Manual, 2^(nd) Ed. (1989) Cold Spring Harbor Laboratory Press).

Another suitable method of creating mutant O-methyltransferases of the present invention is based on a procedure described in Noel and Tsai., 3. Cell. Biochem., 40:309-320, 1989. In so doing, the nucleic acids encoding the O-methyltransferase can be synthetically produced using oligonucleotides having overlapping regions, said oligonucleotides being degenerate at specific bases so that mutations are induced.

According to the present invention, nucleic acid sequences encoding a mutated O-methyltransferase can be produced by the methods described herein, or any alternative methods available to the skilled artisan. In designing the nucleic acid sequence of interest, it may be desirable to reengineer the gene for improved expression in a particular expression system. For example, it has been shown that many bacterially derived genes do not express well in plant systems. In some cases, plant-derived genes do not express well in bacteria. This phenomenon may be due to the non-optimal G+C content and/or A+T content of said gene relative to the expression system being used. For example, the very low G+C content of many bacterial genes results in the generation of sequences mimicking or duplicating plant gene control sequences that are highly A+T rich. The presence of A+T rich sequences within the genes introduced into plants (e.g., TATA box regions normally found in promoters) may result in aberrant transcription of the gene(s). In addition, the presence of other regulatory sequences residing in the transcribed mRNA (e.g. polyadenylation signal sequences (AAUAAA) or sequences complementary to small nuclear RNAs involved in pre-mRNA splicing) may lead to RNA instability. Therefore, one goal in the design of genes is to generate nucleic acid sequences that have a G+C content that affords mRNA stability and translation accuracy for a particular expression system.

Due to the plasticity afforded by the redundancy of the genetic code (i.e., some amino acids are specified by more than one codon), evolution of the genomes of different organisms or classes of organisms has resulted in differential usage of redundant codons. This “codon bias” is reflected in the mean base composition of protein coding regions. For example, organisms with relatively low G+C contents utilize codons having A or T in the third position of redundant codons, whereas those having higher G+C contents utilize codons having G or C in the third position. Therefore, in reengineering genes for expression, one may wish to determine the codon bias of the organism in which the gene is to be expressed. Looking at the usage of the codons as determined for genes of a particular organism deposited in GenBank can provide this information. After determining the bias thereof, the new gene sequence can be analyzed for restriction enzyme sites as well as other sites that could affect transcription such as exon:intron junctions, polyA addition signals, or RNA polymerase termination signals.

Genes or polynucleotide sequences encoding O-methyltransferases, such as ChOMT or IOMT can be placed in an appropriate vector, depending on the artisan's interest, and can be expressed using a suitable expression system. An expression vector, as is well known in the art, typically includes elements that permit replication of said vector within the host cell and may contain one or more phenotypic markers for selection of cells containing the gene. The expression vector will typically contain sequences that control expression such as promoter sequences, ribosome binding sites, and translational initiation and termination sequences. Expression vectors may also contain elements such as subgenomic promoters, a repressor gene or various activator genes. The artisan may also choose to include nucleic acid sequences that result in secretion of the gene product, movement of said product to a particular organelle such as a plant plastid (see U.S. Pat. Nos. 4,762,785; 5,451,513 and 5,545,817, which are incorporated herein by reference) or other sequences that increase the ease of peptide purification, such as an affinity tag.

A wide variety of expression control sequences are useful in expressing native or mutated O-methyltransferases when operably linked thereto. Such expression control sequences include, for example, the early and late promoters of SV40 for animal cells, the lac system, the trp system, major operator and promoter systems of phage S, and the control regions of coat proteins, particularly those from RNA viruses in plants. In E. coli, a useful transcriptional control sequence is the T7 RNA polymerase binding promoter, which can be incorporated into a pET vector as described by Studier et al., Methods Enzymology, 185:60-89, 1990, which is incorporated herein by reference.

For expression, a desired gene should be operably linked to the expression control sequence and maintained in the appropriate reading frame to permit production of the desired O-methyltransferase. Any of a wide variety of well-known expression vectors are of use to the present invention. These include, for example, vectors comprising segments of chromosomal, non-chromosomal and synthetic DNA sequences such as those derived from SV40, bacterial plasmids including those from E. coli such as col E1, pCR1, pBR322 and derivatives thereof, pMB9, wider host range plasmids such as RP4, phage DNA such as phage S, NM989, M13, and other such systems as described by Sambrook et al., (Molecular Cloning, A Laboratory Manual, 2^(nd) Ed. (1989) Cold Spring Harbor Laboratory Press), which is incorporated herein by reference.

A wide variety of host cells are available for expressing O-methyltransferase mutants of the present invention. Such host cells include, for example, bacteria such as E. coli, Bacillus and Streptomyces, fungi, yeast, animal cells, plant cells, insect cells, and the like. Preferred embodiments of the present invention include ChOMT or IOMT mutants that are expressed in E. coli or in plant cells. The plant cells can either be in suspension culture or a transgenic plant.

In order to produce transgenic plants, vectors containing the nucleic acid construct encoding an O-methyltransferase or mutants thereof are inserted into the plant genome. Preferably, these recombinant vectors are capable of stable integration into the plant genome. One variable in making a transgenic plant is the choice of a selectable marker. A selectable marker is used to identify transformed cells against a high background of untransformed cells. The preference for a particular marker is at the discretion of the artisan, but any of the selectable markers may be used along with any other gene not listed herein that could function as a selectable marker. Such selectable markers include aminoglycoside phosphotransferase gene of transposon Tn5 (Aph 11) (which encodes resistance to the antibiotics kanamycin), genes encoding resistance to neomycin or G418, as well as those genes which encode resistance or tolerance to glyphosate, hygromycin, methotrexate, phosphinothricin, imidazolinones, sulfonylureas, triazolophyrimidine herbicides, such as chlorosulfuron, bromoxynil, dalapon, and the like. In addition to a selectable marker, it may be desirable to use a reporter gene. In some instances a reporter gene may be used with a selectable marker. Reporter genes allow the detection of transformed cells and may be used at the discretion of the artisan. A list of these reporter genes is provided in K. Wolsing et al., Ann. Rev. Genetics, 22:421, 1988.

The genes are expressed either by promoters expressing in all tissues at all times (constitutive promoters), by promoters expressing in specific tissues (tissue-specific promoters), promoters expressing at specific stages of development (developmental promoters), and/or promoters expressing in response to a stimulus or stimuli (inducible promoters). The choice of these is at the discretion of the artisan.

Several techniques exist for introducing foreign genes into plant cells, and for obtaining plants that stably maintain and express the introduced gene. Such techniques include acceleration of genetic material coated on a substrate directly into cells (U.S. Pat. No. 4,945,050 to Comell): Plant cells may also be transformed using Agrobacterium technology (see, for example, U.S. Pat. Nos. 5,177,010 to University of Toledo, 5,104,310 to Texas A&M, U.S. Pat. Nos. 5,149,645, 5,469,976, 5,464,763, 4,940,838, and 4,693,976 to Schilperoot, European Patent Applications 116718, 290799, 320500 to Max Planck, European Patent Applications 604662, 627752 and U.S. Pat. No. 5,591,616 to Japan Tobacco, European Patent Applications 0267159, 0292435 and U.S. Pat. No. 5,231,011 to Ciba-Geigy, U.S. Pat. Nos. 5,463,174 and 4,762,785 to Calgene, and U.S. Pat. Nos. 5,004,863 and 5,159,135 to Agracetus). Other transformation technologies include whiskers technology (see U.S. Pat. Nos. 5,302,523 and 5,464,765 to Zeneca). Electroporation technology has also been used to transform plants (see WO 87106614 to Boyce Thompson Institute, 5,472,869 and 5,384,253 to Dakalb, and WO 92/09696 and WO 93/21335 to Plant Genetic Systems, all which are incorporated by reference). Viral vector expression systems can also be used such as those described in U.S. Pat. Nos. 5,316,931, 5,589,367, 5,811,653, and 5,866,785 to BioSource, which are incorporated herein by reference.

In addition to numerous technologies for transforming plants, the type of tissue that is contacted with the genes of interest may vary as well. Suitable tissue includes, for example, embryonic tissue, callus tissue, hypocotyl, meristem, and the like. Almost all plant tissues may be transformed during de-differentiation using the appropriate techniques described herein.

Regardless of the transformation system used, a gene encoding a mutant O-methyltransferase is preferably incorporated into a gene transfer vector adapted to express said gene in a plant cell by including in the vector an expression control sequence (e.g., a plant promoter regulatory element). In addition to plant promoter regulatory elements, promoter regulatory elements from a variety of sources can be used efficiently in plant cells to express foreign genes. For example, promoter regulatory elements of bacterial origin, such as the octopine synthase promoter, the nopaline synthase promoter, the mannopine synthase promoter, and the like, may be used. Promoters of viral origin, such as the cauliflower mosaic virus (35S and 198) are also desirable. Plant promoter regulatory elements also include ribulose-1,6-bisphosphate carboxylase small subunit promoter, beta-conglycinin promoter, phaseolin promoter, ADH promoter, heat-shock promoters, tissue specific promoters, and the like. Numerous promoters are available to skilled artisans for use at their discretion.

It should be understood that not all expression vectors and expression systems function in the same way to express the mutated gene sequences of the present invention. Neither do all host cells function equally well with the same expression system. However, one skilled in the art may make a selection among these vectors, expression control sequences, and host without undue experimentation and without departing from the scope of this invention.

Once an O-methyltransferase of the present invention is expressed, the protein obtained therefrom can be purified so that structural analysis, modeling, and/or biochemical analysis can be performed, as exemplified herein. The nature of the protein obtained can be dependent on the expression system used. For example, genes, when expressed in mammalian or other eukaryotic cells, may contain latent signal sequences that may result in glycosylation, phosphorylation, or other post-translational modifications, which may or may not alter function. Therefore, a preferred embodiment of the present invention is the expression of mutant O-methyltransferase genes in E. coli cells. Once the proteins are expressed, they can be easily purified using techniques common to the person having ordinary skill in the art of protein biochemistry, such as, for example, techniques described in Colligan at al., (1997) Current Protocols in Protein Science, Chanda, V. B., Ed., John Wiley & Sons, Inc., which is incorporated herein by reference. Such techniques often include the use of cation-exchange or anion-exchange chromatography, gel filtration-size exclusion chromatography, and the like. Another technique that may be commonly used is affinity chromatography. Affinity chromatography can include the use of antibodies, substrate analogs, or histidine residues (His-tag technology).

Once purified, mutants of the present invention may be characterized by any of several different properties. For example, such mutants may have altered active site surface charges of one or more charge units. In addition, the mutants may have altered substrate specificity or product capability relative to a non-mutated O-methyltransferase (e.g., a ChOMT or IOMT).

The present invention allows for the characterization of O-methyltransferase mutants by crystallization followed by X-ray diffraction. Polypeptide crystallization occurs in solutions where the polypeptide concentration exceeds it solubility maximum (i.e., the polypeptide solution is supersaturated). Such solutions may be restored to equilibrium by reducing the polypeptide concentration, preferably through precipitation of the polypeptide crystals. Often polypeptides may be induced to crystallize from supersaturated solutions by adding agents that alter the polypeptide surface charges or perturb the interaction between the polypeptide and bulk water to promote associations that lead to crystallization.

Compounds known as “precipitants” are often used to decrease the solubility of the polypeptide in a concentrated solution by forming an energetically unfavorable precipitating layer around the polypeptide molecules (Weber, Advances in Protein to Chemistry, 41:1-36, 1991). In addition to precipitants, other materials are sometimes added to the polypeptide crystallization solution. These include buffers to adjust the pH of the solution and salts to reduce the solubility of the polypeptide. Various precipitants are known in the art and include the following: ethanol, 3-ethyl-2,4-pentanediol, many of the polyglycols (such as polyethylene glycol), and the like.

Commonly used polypeptide crystallization methods include the following techniques: batch, hanging drop, seed initiation, dialysis, and the like. In each of these methods, it is important to promote continued crystallization after nucleation by maintaining a supersaturated solution. In the batch method, polypeptide is mixed with precipitants to achieve supersaturation, the vessel is sealed, and set aside until crystals appear. In the dialysis method, polypeptide is retained in a sealed dialysis membrane that is placed into a solution containing precipitant. Equilibration across the membrane increases the polypeptide and precipitant concentrations thereby causing the polypeptide to reach supersaturation levels.

In the preferred hanging drop technique (McPherson, J. Biol. Chem., 6300-6306, 1976), an initial polypeptide mixture is created by adding a precipitant to a concentrated polypeptide solution. The concentrations of the polypeptide and precipitants are such that in this initial form, the polypeptide does not crystallize. A small drop of this mixture is placed on a glass slide that is inverted and suspended over a reservoir of a second solution. The system is then sealed. Typically, the second solution contains a higher concentration of precipitant or other dehydrating agent. The difference in the precipitant concentrations causes the protein solution to have a higher vapor pressure than the solution. Since the system containing the two solutions is sealed, an equilibrium is established, and water from the polypeptide mixture transfers to the second solution. This equilibrium increases the polypeptide and precipitant concentration in the polypeptide solution. At the critical concentration of polypeptide and precipitant, a crystal of the polypeptide will form.

Another method of crystallization involves introducing a nucleation site into a concentrated polypeptide solution. Generally, a concentrated polypeptide solution is prepared and a seed crystal of the polypeptide is introduced into this solution. If the concentration of the polypeptide and any precipitants are correct, the seed crystal will provide a nucleation site around which a larger crystal forms. In typical embodiments, the crystals of the present invention are formed in hanging drops with a solution comprising 10-20% PEG 8000; 200-400 mM of an ammonium or lithium salt, and 2 mM dithiothreitol as precipitant.

Some proteins may be recalcitrant to crystallization. However, several techniques are available to the skilled artisan. Quite often the removal of polypeptide segments at the amino or carboxy terminal end of the protein is necessary to produce crystalline protein samples. Said procedures involve either treatment of the protein with one of several proteases including trypsin, chymotrypsin, substilisin, and the like. This treatment often results in the removal of flexible polypeptide segments that are likely to negatively affect crystallization. Alternatively, the removal of coding sequences from the protein's gene facilitates the recombinant expression of shortened proteins that can be screened for crystallization.

The crystals so produced have a wide range of uses. For example, high quality crystals are suitable for X-ray or neutron diffraction analysis to determine the three-dimensional structure of mutant and native O-methyltransferases and to design additional mutants thereof. In addition, crystallization can serve as a further purification method. In some instances, a polypeptide or protein will crystallize from a heterogeneous mixture into crystals. Isolation of such crystals by filtration, centrifugation, etc., followed by redissolving the polypeptide affords a purified solution suitable for use in growing the high-quality crystals needed for diffraction studies. The high-quality crystals may also be dissolved in water and then formulated to provide an aqueous solution having other uses as desired.

Because O-methyltransferases may crystallize in more than one crystal form, the structural coordinates of alpha-carbons of an active site determined from an O-methyltransferase (e.g., ChOMT or IOMT) or portions thereof, as provided by this invention, are particularly useful to solve the structure of other crystal forms of O-methyltransferases. The structural coordinates, as provided herein, may also be used to solve the structure of O-methyltransferases having alpha-carbons positioned within the active sites in a manner similar to the wild-type O-methyltransferase, yet having R-groups that may or may not be identical to the wild-type O-methyltransferase.

Furthermore, the structural coordinates disclosed herein may be used to determine the structure of the crystalline form of other proteins with significant amino acid or structural homology to any functional domain of an O-methyltransferase. One method that may be employed for such purpose is molecular replacement. In this method, the unknown crystal structure, whether it is another crystal form of an O-methyltransferase, an O-methyltransferase having a mutated active site, or the crystal of some other protein with significant sequence and/or structural homology to an O-methyltransferase may be determined using the coordinates given in Appendices A-D. This method provides sufficient structural form for the unknown crystal more efficiently than attempting to determine such information ab initio. In addition, this method can be used to determine whether or not a given O-methyltransferase in question falls within the scope of this invention.

As further disclosed herein, O-methyltransferases and mutants thereof may be crystallized in the presence or absence of substrates and substrate analogs. The crystal structures of a series of complexes may then be solved by molecular replacement and compared to that of the wild-type O-methyltransferase to assist in determination of suitable replacements for R-groups within the active site, thus making O-methyltransferase mutants according to the present invention.

All mutants of the present inventions may be modeled using the information disclosed herein without necessarily having to crystallize and solve the structure for each and every mutant. For example, one skilled in the art may use one of several specialized computer programs to assist in the process of designing O-methyltransferases having mutated active sites relative to the wild-type O-methyltransferase. Examples of such programs include: GRID (Goodford, 1985, J. Mod. Chem., 28:849-857), MCSS (Miranker and Karplus, 1991, Proteins: Structure, Function and Genetics, 11:29-34); AUTODOCK (Goodsell and Olsen, 1990, Proteins. Structure, Fumtion, and Genetics, 8:195-202); and DOCK (Kuntz et al., 1982, J. Mot Biol., 161:269-288), and the like, as well as those discussed in the Examples below. In addition, specific computer programs are also available to evaluate specific substrate-active site interactions and the deformation energies and electrostatic interactions resulting therefrom. MODELLER is a computer program often used for homology or comparative modeling of the three-dimensional structure of a protein. A. Saii & T. L. Blundell. J. Mol. Biol. 234:779-815, 1993. A sequence to be modeled is aligned with one or more known related structures and the MODELLER program is used to calculate a full-atom model, based on optimum satisfaction of spatial restraints. Such restraints can include, inter alia, homologous structures, site-directed mutagenesis, fluorescence spectroscopy, NMR experiments, or atom-atom potentials of mean force.

The present invention enables O-methyltransferase mutants to be made and the crystal structure thereof to be solved. Moreover, by virtue of the present invention, the location of the active site and the interface of substrate therewith permit the identification of desirable R-groups for introduction by mutagenesis.

The three-dimensional coordinates of the O-methyltransferases provided herein may additionally be used to predict the activity and/or substrate specificity of a protein whose primary amino acid sequence suggests that it may have O-methyltransferase activity. The family of O-methyltransferase-related enzymes is defined, in part, by a number of conserved amino acid residues including, for example, the residues identified in FIG. 5B. By employing the three-dimensional coordinates disclosed herein and computer modeling programs, structural comparisons of O-methyltransferases such as ChOMT or IOMT can be made with a putative enzyme. Similarities and/or differences between the two would provide the skilled artisan with information regarding the activity and/or substrate specificity of the putative enzyme.

Thus, in another embodiment of the invention, there is provided a method of predicting the activity and/or substrate specificity of an O-methyltransferase or putative O-methyltransferase comprising (a) generating a three-dimensional representation of a known O-methyltransferase (e.g., ChOMT or IOMT) using three-dimensional coordinate data, (b) generating a predicted three-dimensional representation of a putative O-methyltransferase, and (c) comparing the representation of the known O-methyltransferase with the representation of the putative O-methyltransferase, wherein the similarities and/or differences between the two representations are predictive of activity and/or substrate specificity of the putative O-methyltransferase.

In a further embodiment of the present invention, there is also provided a method of identifying a potential substrate of an O-methyltransferase comprising (a) defining the active site of an O-methyltransferase (e.g., ChOMT or IOMT) based on the atomic coordinates of the O-methyltransferase, (b) identifying a potential substrate that fits the defined active site, and (c) contacting the O-methyltransferase with the potential substrate of (b) and determining the activity thereon. Techniques for computer modeling and structural comparisons similar to those described herein for predicting putative O-methyltransferase activity and/or substrate specificity can be used to identify novel substrates for O-methyltransferases.

In addition, the structural coordinates and three-dimensional models disclosed herein can be used to design or identify O-methyltransferase inhibitors. Using the modeling techniques disclosed herein, potential inhibitor structures can be modeled with the O-methyltransferase active site and those that appear to interact therewith can subsequently be tested in activity assays in the presence of substrate.

Methods of using crystal structure data to design binding agents or substrates to are known in the art. Thus, the crystal structure data provided herein can be used in the design of new or improved inhibitors, substrates or binding agents. For example, the O-methyltransferase polypeptide coordinates can be superimposed onto other available coordinates of similar enzymes to identify modifications in the active sites of the enzymes to create novel by-products of enzymatic activity or to modulate phenylpropanoid synthesis. Alternatively, the O-methyltransferase polypeptide coordinates can be superimposed onto other available coordinates of similar enzymes which have substrates or inhibitors bound to them to give an approximation of the way these and related substrates or inhibitors might bind to an O-methyltransferase. Alternatively, computer programs employed in the practice of rational drug design can be used to identify compounds that reproduce interaction characteristics similar to those found between an O-methyltransferase polypeptide and a co-crystallized substrate. Furthermore, detailed knowledge of the nature of binding site interactions allows for the modification of compounds to alter or improve solubility, pharmacokinetics, etc. without affecting binding activity.

Computer programs are widely available that are capable of carrying out the activities necessary to design agents using the crystal structure information provided herein. Examples include, but are not limited to, the computer programs listed below:

-   -   Catalyst Databases™—an information retrieval program accessing         chemical databases such as BioByte Master File, Derwent WDI and         ACD;     -   Catalyst/HYPO™—generates models of compounds and hypotheses to         explain variations of activity with the structure of drug         candidates;     -   Ludi™—fits molecules into the active site of a protein by         identifying and matching complementary polar and hydrophobic         groups;     -   Leapfrog™—“grows” new ligands using a genetic algorithm with         parameters under the control of the user.

In addition, various general-purpose machines may be used with programs written in accordance with the teachings herein, or it may be more convenient to construct more specialized apparatus to perform the operations. However, preferably the embodiment is implemented in one or more computer programs executing on programmable systems each comprising at least one processor, at least one data storage system (including volatile and non-volatile memory and/or storage elements), at least one input device, and at least one output device. The program is executed on the processor to perform the functions described herein.

Each such program may be implemented in any desired computer language (including machine, assembly, high level procedural, object oriented programming languages, or the like) to communicate with a computer system. In any case, the language may be a compiled or interpreted language. The computer program will typically be stored on a storage media or device (e.g., ROM, CD-ROM, or magnetic or optical media) readable by a general or special purpose programmable computer, for configuring and operating the computer when the storage media or device is read by the computer to perform the procedures described herein. The system may also be considered to be implemented as a computer-readable storage medium, configured with a computer program, where the storage medium so configured causes a computer to operate in a specific and predefined manner to perform the functions described herein.

Embodiments of the invention include systems (e.g., internet based systems), particularly computer systems that store and manipulate the coordinate and sequence information described herein. One example of a computer system 100 is illustrated in block diagram form in FIG. 8. As used herein, “a computer system” refers to the hardware components, software components, and data storage components used to analyze the coordinates and sequences as set forth in Tables 1 (SEQ ID NO: 1 and 2) and Table 2 (SEQ ID NO: 3 and 4), Appendices A-D and PDB Accession Nos. 1FPQ, 1FP1, 1FPX, 1FP2. The computer system 100 typically includes a processor for processing, accessing and manipulating the sequence data. The processor 105 can be any well-known type of central processing unit, such as, for example, the Pentium III from Intel Corporation, or similar processor from Sun, Motorola, Compaq, AMD or International Business Machines.

Typically the computer system 100 is a general purpose system that comprises the processor 105 and one or more internal data storage components 110 for storing data, and one or more data retrieving devices for retrieving the data stored on the data storage components. A skilled artisan can readily appreciate that any one of the currently available computer systems are suitable.

In one particular embodiment, the computer system 100 includes a processor 105 connected to a bus which is connected to a main memory 115 (preferably implemented as RAM) and one or more internal data storage devices 110, such as a hard drive and/or other computer readable media having data recorded thereon. In some embodiments, the computer system 100 further includes one or more data retrieving device 118 for reading the data stored on the internal data storage devices 110.

The data retrieving device 118 may represent, for example, a floppy disk drive, a compact disk drive, a magnetic tape drive, or a modem capable of connection to a remote data storage system (e.g., via the internet) etc. In some embodiments, the internal data storage device 110 is a removable computer readable medium such as a floppy disk, a compact disk, a magnetic tape, etc. containing control logic and/or data recorded thereon. The computer system 100 may advantageously include or be programmed by appropriate software for reading the control logic and/or the data from the data storage component once inserted in the data retrieving device.

The computer system 100 includes a display 120, which is used to display output to a computer user. It should also be noted that the computer system 100 can be linked to other computer systems 125 a-c in a network or wide area network to provide centralized access to the computer system 100.

Software for accessing and processing the coordinate and sequences described herein, (such as search tools, compare tools, and modeling tools etc.) may reside in main memory 115 during execution.

For the first time, the present invention permits the use of molecular design techniques to design, select and synthesize novel enzymes, chemical entities and compounds, including inhibitory compounds, capable of binding to an O-methyltransferase polypeptide (e.g., a ChOMT or IOMT polypeptide), in whole or in part.

One approach enabled by this invention is the use of structural coordinates as set forth in Appendices A-D and PDB Accession Nos. 1FPQ, 1FP1, 1FPX, 1FP2 to design new enzymes capable of synthesizing novel phenylpropanoids. For example, O-methyltransferases generate molecular diversity in their products by utilizing different starter molecules. The structural coordinates disclosed herein allow the elucidation of the nature by which O-methyltransferases achieve starter molecule selectivity and control phenylpropanoids diversity and synthesis. Accordingly, the invention allows for the strategic development and biosynthesis of more diverse phenylpropanoid and demonstrates a structural basis for control of phenylpropanoid synthesis. In addition, the structural coordinates allow for the development of substrates or binding agents that bind to the polypeptide and alter the physical properties of the compounds in different ways, e.g., solubility.

In another approach an O-methyltransferase polypeptide crystal is probed with molecules composed of a variety of different chemical entities to determine optimal sites for interaction between candidate binding molecules (e.g., substrates) and the O-methyltransferase (e.g., ChOMT or IOMT).

In another embodiment, an approach made possible and enabled by this invention is to screen computationally small molecule databases for chemical entities or compounds that can bind in whole, or in part, to an O-methyltransferase polypeptide or fragment thereof. In this screening, the quality of fit of such entities or compounds to the binding site may be judged either by shape complementarity or by estimated interaction energy. Meng, E. C. et al., J. Comp. Chem., 13, pp. 505-524 (1992).

ChOMT and IOMT are two members of a family of O-methyltransferase polypeptides, many of which have similar functional activity. In addition, many O-methyltransferase polypeptides may crystallize in more than one crystal form. Accordingly, the structural coordinates of ChOMT or IOMT, or portions thereof, as provided by this invention are particularly useful to solve the structure, function or activity of other crystal forms of O-methyltransferase polypeptides. They may also be used to solve the structure of an O-methyltransferase mutant.

One method that may be employed for this purpose is molecular replacement. In this method, the unknown crystal structure, whether it is another O-methyltransferase crystal form, O-methyltransferase, O-methyltransferase mutant, an O-methyltransferase complexed with a substrate or other molecule, or the crystal of some other protein with significant amino acid sequence homology to any O-methyltransferase polypeptide, may be determined using the structure coordinates as provided in Appendices A-D and PDB Accession Nos. 1FPQ, 1FP1, 1FPX, 1FP2. This method will provide an accurate structural form for the unknown crystal more quickly and efficiently than attempting to determine such information ab initio.

In addition, in accordance with the present invention, an O-methyltransferase or O-methyltransferase mutant may be crystallized in association or complex with known O-methyltransferase binding agents, substrates, or inhibitors. The crystal structures of a series of such complexes may then be solved by molecular replacement and compared with that of wild-type O-methyltransferase polypeptides. Potential sites for modification within the O-methyltransferase polypeptide may thus be identified. This information provides an additional tool for determining the most efficient binding interactions between an O-methyltransferase and a chemical entity, substrate or compound.

All of the complexes referred to above may be studied using well-known X-ray diffraction techniques and may be refined to 2-3 angstrom resolution X-ray data to an R value of about 0.20 or less using computer software, such as X-PLOR (Yale University, 1992, distributed by Molecular Simulations, Inc.). See, e.g., Blundel & Johnson, supra; Methods in Enzymology, vol. 114 and 115, H. W. Wyckoff et al., eds., Academic Press (1985). This information may thus be used to optimize known classes of O-methyltransferase substrates or binding agents (e.g., inhibitors), and to design and synthesize novel classes of O-methyltransferases, substrates, and binding agents (e.g., inhibitors).

The design of substrates, compounds or binding agents that bind to or inhibit an O-methyltransferase polypeptide according to the invention generally involves consideration of two factors. First, the substrate, compound or binding agent must be capable of physically and structurally associating with the O-methyltransferase polypeptide. Non-covalent molecular interactions important in the association of an O-methyltransferase with a substrate include hydrogen bonding, van der Waals and hydrophobic interactions, and the like.

Second, the substrate, compound or binding agent must be able to assume a conformation that allows it to associate with an O-methyltransferase polypeptide. Although certain portions of the substrate, compound or binding agent will not directly participate in this association, those portions may still influence the overall conformation of the molecule. This, in turn, may have a significant impact on potency. Such conformational requirements include the overall three-dimensional structure and orientation of the chemical entity or compound in relation to all or a portion of the binding site, e.g., active site or accessory binding site of an O-methyltransferase (e.g., a ChOMT or IOMT polypeptide), or the spacing between functional groups of a substrate or compound comprising several chemical entities that directly interact with an O-methyltransferase.

The potential binding effect of a substrate or chemical compound on an O-methyltransferase or the activity of a newly synthesized or mutated O-methyltransferase might have on a known substrate may be analyzed prior to its actual synthesis and testing by the use of computer modeling techniques. For example, if the theoretical structure of the given substrate or compound suggests insufficient interaction and association between it and an O-methyltransferase, synthesis and testing of the compound may not be warranted. However, if computer modeling indicates a strong interaction, the molecule may then be tested for its ability to bind to and initiate catalysis of a substrate by an O-methyltransferase. Methods of assaying for O-methyltransferase activity are known in the art (as identified and discussed herein). Methods for assaying the effect of a newly created O-methyltransferase or a potential substrate or binding agent can be performed in the presence of a known binding agent of O-methyltransferase. For example, the effect of the potential binding agent can be assayed by measuring the ability of the potential binding agent to compete with a known substrate.

A mutagenized O-methyltransferase, novel O-methyltransferase, substrate or other binding compound of an O-methyltransferase may be computationally evaluated and designed by means of a series of steps in which chemical entities or fragments are screened and selected for their ability to associate with the individual binding pockets or other areas of the O-methyltransferase.

One skilled in the art may use one of several methods to screen chemical entities or fragments for their ability to associate with an O-methyltransferase and more particularly with the individual binding pockets of an O-methyltransferase polypeptide. This process may begin by visual inspection of, for example, the active site on the computer screen based on the coordinates in Appendices A-D and Accession Nos. 1FPQ, 1FP1, 1FPX, 1FP2. Selected fragments or substrates or chemical entities may then be positioned in a variety of orientations, or docked, within an individual binding pocket of an O-methyltransferase. Docking may be accomplished using software such as Quanta and Sybyl, followed by energy minimization and molecular dynamics with standard molecular mechanics forcefields, such as CHARMM and AMBER.

Specialized computer programs may also assist in the process of selecting fragments or chemical entities. These include:

1. GRID (Goodford, P. J., “A Computational Procedure for Determining Energetically Favorable Binding Sites on Biologically Important Macromolecules”, J. Med. Chem., 28, pp. 849-857 (1985)). GRID is available from Oxford University, Oxford, UK.

2. MCSS (Miranker, A. and M. Karpl, “Functionality Maps of Binding Sites: A Multiple Copy Simultaneous Search Method.” Proteins: Structure. Function and Genetics, 11, pp. 29-34 (1991)). MCSS is available from Molecular Simulations, Burlington, Mass.

3. AUTODOCK (Goodsell, D. S, and A. J. Olsen, “Automated Docking of Substrates to Proteins by Simulated Annealing”, Proteins: Structure. Function, and Genetics, 8, pp. 195-202 (1990)). AUTODOCK is available from Scripps Research institute, La Jolla, Calif.

4. DOCK (Kuntz, I. D. et al., “A Geometric Approach to Macromolecule-Ligand Interactions”, J. Mol. Biol., 161, pp. 269-288 (1982)). DOCK is available from University of California, San Francisco, Calif.

Once suitable substrates, chemical entities or fragments have been selected, they can be assembled into a single polypeptide, compound or binding agent (e.g., an inhibitor). Assembly may be performed by visual inspection of the relationship of the fragments to each other on the three-dimensional image displayed on a computer screen in relation to the structure coordinates of the molecules as set forth in Appendices A-D and Accession Nos. 1FPQ, 1FP 1, 1FPX, 1FP2. This would be followed by manual model building using software such as Quanta or Sybyl.

Useful programs to aid one of skill in the art in connecting the individual chemical entities or fragments include:

1. CAVEAT (Bartlett, P. A. et al, “CAVEAT: A Program to Facilitate the Structure-Derived Design of Biologically Active Molecules”. In “Molecular Recognition in Chemical and Biological Problems”, Special Pub., Royal Chem. Soc., 78, pp. 182-196 (1989)). CAVEAT is available from the University of California, Berkeley, Calif.

2. 3D Database systems such as MACCS-3D (MDL Information Systems, San Leandro, Calif.). This area is reviewed in Martin, Y. C., “3D Database Searching in Drug Design”, J. Med. Chem., 35, pp. 2145-2154 (1992)).

3. HOOK (available from Molecular Simulations, Burlington, Mass.).

In addition to the method of building or identifying novel enzymes or an O-methyltransferase substrate or binding agent in a step-wise fashion one fragment or chemical entity at a time as described above, substrates, inhibitors or other enzymatic interactions may be designed as a whole or “de novo” using either an empty active site or optionally including some portion(s) of known substrates, binding agents or inhibitors. These methods include:

1. LUDI (Bohm, H.-J., “The Computer Program LUDI: A New Method for the De Novo Design of Enzyme Inhibitors”, J. Comp. Aid. Mol. Design, 6, pp. 61-78 (1992)). LUDI is available from Biosym Technologies, San Diego, Calif.

2. LEGEND (Nishibata, Y. and A. Itai, Tetrahedron, 47, p. 8985 (1991)). LEGEND is available from Molecular Simulations, Burlington, Mass.

3. LeapFrog (available from Tripos Associates, St. Louis, Mo.).

Other molecular modeling techniques may also be employed in accordance with this invention. See, e.g., Cohen, N. C. et al., “Molecular Modeling Software and Methods for Medicinal Chemistry”, J. Med. Chem., 33, pp. 883-894 (1990). See also, Navia, M. A. and M. A. Murcko, “The Use of Structural Information in Drug Design”, Current Opinions in Structural Biology, 2, pp. 202-210 (1992).

Once a substrate, compound or binding agent has been designed or selected by the above methods, the efficiency with which that substrate, compound or binding agent may bind to an O-methyltransferase may be tested and optimized by computational evaluation.

A substrate or compound designed or selected as an O-methyltransferase binding agent may be further computationally optimized so that in its bound state it would preferably lack repulsive electrostatic interaction with the target site. Such non-complementary (e.g., electrostatic) interactions include repulsive charge-charge, dipole-dipole and charge-dipole interactions. Specifically, the sum of all electrostatic interactions between the binding agent and the O-methyltransferase polypeptide when the binding agent is bound to the enzyme, preferably make a neutral or favorable contribution to the enthalpy of binding.

Specific computer software is available in the art to evaluate compound deformation energy and electrostatic interaction. Examples of programs designed for such uses include: Gaussian 92, revision C (M. J. Frisch, Gaussian, Inc., Pittsburgh, Pa., 1992); AMBER, version 4.0 (P. A. Kollman, University of California at San Francisco, 1994); QUANTA/CHARMM (Molecular Simulations, Inc., Burlington, Mass. 1994); and Insight II/Discover (Biosysm Technologies Inc., San Diego, Calif., 1994). These programs may be implemented, for example, using a Silicon Graphics workstation, IRIS 4D/35 or IBM RISC/6000 workstation model 550. Other hardware systems and software packages will be known to those skilled in the art of which the speed and capacity are continually modified.

Once an O-methyltransferase, O-methyltransferase substrate or O-methyltransferase binding agent has been selected or designed, as described above, substitutions may then be made in some of its atoms or side groups in order to improve or modify its binding properties. Generally, initial substitutions are conservative, e.g., the replacement group will have approximately the same size, shape, hydrophobicity and charge as the original group. Such substituted chemical compounds may then be analyzed for efficiency of fit to an O-methyltransferase substrate or fit of a modified substrate to an O-methyltransferase having a structure defined by the coordinates in Appendices A-D and Accession Nos. 1FPQ, 1FP1, 1FPX, 1FP2, by the same computer methods described, above.

Conserved regions of the O-methyltransferase family of enzymes lend to themselves to the methods and compositions of the invention. For example, a number of O-methyltransferases have conserved residues present within their amino acid sequence (as described more fully below). Accordingly, modification to the active site or amino acid sequence of ChOMT or IOMT or a ChOMT or IOMT substrate can be extrapolated to other conserved members of the family of O-methyltransferases.

Functional fragments of O-methyltransferase polypeptides such as, for example, fragments of ChOMT and IOMT, can be designed based on the crystal structure and atomic coordinates described herein. Fragments of a ChOMT and IOMT polypeptide and the fragment's corresponding atomic coordinates can be used in the modeling described herein. In addition, such fragments may be used to design novel substrates or modified active sites to create new diverse phenylpropanoid compounds.

In one embodiment of the present invention, the crystal structure and atomic coordinates allow for the design of novel O-methyltransferases and novel O-methyltransferase substrates. The development of new O-methyltransferases will lead to the development of a biodiverse library of phenylpropanoid compounds for use as therapeutics (e.g., as antibiotics, anti-cancer agents, anti-fungal agents) as described herein or known in the art. In vitro assay systems for production and determination of activity are known in the art. For example, antibiotic activities of novel products of the polyketide pathway, flavonoid pathway, and phenylpropanoid pathway can be measured by any number of anti-microbial techniques currently used in hospitals and laboratories. In addition, anticancer activity can be determined by contacting cells having a cell proliferative disorder with a newly synthesized phenylpropanoid compound and measuring the proliferation or apoptosis of the cells before and after contact with a phenylpropanoid. Specific examples of apoptosis assays are provided in the following references: Lymphocyte: C. 3. Li et al., Science, 268:429-431, 1995; D. Gibellini et al., Br. J. Haematol. 89:24-33, 1995; S. J. Martin et al., J. Immunol. 152:330-42, 1994; C. Terai et al., 3. Clin Invest. 87:1710-5, 1991; J. Dhein et al., Nature 373:438-441, 1995; P. D. Katsikis et al., J. Exp. Med. 1815:2029-2036, 1995; Michael O. Westendorp et al., Nature 375:497, 1995; DeRossi et al., Virology 198:234-44, 1994. Fibroblasts: H. Vossbeck et al., hit. J. Cancer 61:92-97, 1995; S. Goruppi et al., Oncogene 9:1537-44, 1994; A. Fernandez et al., Oncogene 9:2009-17, 1994; E. A. Harrington et al., EMBO J. 13:3286-3295, 1994; N. Itoh et al., J. Biol. Chem. 268:10932-7, 1993. Neuronal Cells: G. Melino et al., Mol. Cell. Biol. 14:6584-6596, 1994; D. M. Rosenbaum et al., Ann. Neurol. 36:864-870, 1994; N. Sato et al., J. Neurobiol 25:1227-1234, 1994; G. Ferrari et al., J. Neurosci. 1516:2857-2866, 1995; A. K. Talley et al., Mol. Cell. Biol. 1585:2359-2366, 1995; A. K. Talley et al., Mol. and Cell. Biol. 15:2359-2366, 1995; G. Walkinshaw et al., J. Clin. Invest. 95:2458-2464, 1995. Insect Cells: R. J. Clein et al., Science 254:1388-90, 1991; N. E. Crook et al., J. Virol. 67:2168-74, 1993; S. Rabizadeh et al., J. Neurochem. 61:2318-21, 1993; M. J. Birnbaum et al., J. Virol 68:2521-8, 1994; R. J. Clem et al., Mol. Cell. Biol. 14:5212-5222, (1994). Other assays are well within the ability of those of skill in the art.

Production of novel phenylpropanoid or O-methyltransferases can be carried out in culture. For example, mammalian expression constructs carrying O-methyltransferases can be introduced into various cell lines such as CHO, 3T3, HL60, Rat-1, or Jurkart cells, for example. In addition, SF21 insect cells may be used in which case the O-methyltransferase polynucleotide is expressed using an insect heat shock promoter.

In another embodiment of the present invention, once a novel substrate or binding agent is developed by the computer methodology discussed above, the invention provides a method for determining the ability of the substrate or agent to be acted upon by an O-methyltransferase. The method includes contacting components comprising the substrate or agent and an O-methyltransferase, or a recombinant cell expressing an O-methyltransferase, under conditions sufficient to allow the substrate or agent to interact and determining the affect of the agent on the activity of the polypeptide. The term “affect”, as used herein, encompasses any means by which protein activity can be modulated, and includes measuring the interaction of the agent with the O-methyltransferase polypeptide by physical means including, for example, fluorescence detection of the binding of an agent to the polypeptide. Such agents can include, for example, polypeptides, peptidomimetics, chemical compounds, small molecules, substrates and biologic agents as described herein. Examples of small molecules include but are not limited to small peptides or peptide-like molecules.

Contacting or incubating includes conditions that allow contact between the test agent or substrate and an O-methyltransferase or modified O-methyltransferase polypeptide or a cell expressing an O-methyltransferase or modified O-methyltransferase polypeptide. Contacting includes in solution and in solid phase. The substrate or test agent may optionally be a combinatorial library for screening a plurality of substrates or test agents. Agents identified in the method of the invention can be further evaluated by chromatography, cloning, sequencing, and the like.

Although methods and materials similar or equivalent to those described herein can be used to practice the invention, suitable methods and materials are described below. All publications, patent applications, patents and other references mentioned herein are incorporated by reference in their entirety. The invention will now be described in greater detail by reference to the following non-limiting examples.

EXAMPLES

Expression, purification, and mutagenesis. The alfalfa ChOMT gene (accession number AAC49927) and IOMT gene (accession number AAB48059) were inserted into the E. coli expression vector pHIS8 (ChOMT) or pET-15b (IOMT). ChOMT and IOMT constructs were transformed into E. coli BL21(DE3). Transformed E. coli were grown at 37° C. in terrific broth (TB) containing 50 μg ml⁻¹ kanamycin (ChOMT) or 100 μg ml⁻¹ ampicillin (IOMT) until A_(600nm)=1.0. After induction with 0.5 mM isopropyl 1-thio-β-galactopyranoside (IPTG), the cultures were grown for 6 hr at 25° C. Cells were pelleted, harvested, and resuspended in lysis buffer (50 mM Tris-HCl (pH 8.0), 500 mM NaCl, 20 mM imidazole (pH 8.0), 20 mM β-mercaptoethanol, 10% (v/v) glycerol, and 1% (v/v) Tween-20). After sonication and centrifugation, the supernatant was passed over a Ni²⁺-NTA column, washed with 10 bed volumes of lysis buffer, 10 bed volumes of wash buffer (50 mM Tris-HCl (pH 8.0), 500 mM NaCl, 20 mM imidazole (pH 8.0), 20 mM β-mercaptoethanol, and 10% (v/v) glycerol), then the His-tagged protein was eluted with elution buffer (50 mM Tris-HCl (pH 8.0), 500 mM NaCl, 250 mM imidazole (pH 8.0), 20 mM β-mercaptoethanol, and 10% (v/v) glycerol). Incubation with thrombin during dialysis for 24 hr at 4° C. against 25 mM HEPES (pH 7.5), 100 mM NaCl, 1 mM dithiothreitol (DTT) removed the N-terminal His-tag. Dialyzed protein was reloaded onto a Ni²⁺-NTA column to remove cleaved His-tag followed by thrombin depletion using a benzamidine Sepharose column. Gel filtration on a Superdex 200 column equilibrated with 25 mM HEPES (pH 7.5), 100 mM NaCl, 1 mM DTT resulted in homogenous and active ChOMT and IOMT. Fractions containing the protein of interest were pooled and concentrated to approximately 25 mg ml⁻¹ and stored at −80° C. Se-met substituted protein was obtained from E. coli grown in minimal media with appropriate amino acids and seleno-methionine added. Expression and purification steps were as above. All mutants were generated with the QuikChange (Stratagene) protocol. Automated nucleotide sequencing confirmed the fidelity of the PCR products (Salk Institute DNA sequencing facility). All mutants were expressed as described above.

Enzyme Activity Assays. Mutant enzymes were purified by Ni⁺² affinity chromatography, dialyzed against 25 mM HEPES (pH 7.5), 100 mM NaCl, 2 mM DTT, and concentrated to approximately 2 mg ml⁻¹. Qualitative activity assays were performed using 20 μg of protein, 500 μM substrate (2′,4,4′-trihydroxychalcone for ChOMT and 4′,7-dihydroxyisoflavone for IOMT), and 500 μM adenosyl-L-methionine-S-(methyl-¹⁴C), in 50 μl of 250 mM HEPES (pH 7.5), 100 mM NaCl. Reactions were allowed to proceed for 2 hr at room temperature after which time the reaction products were extracted into ethyl acetate and applied to a Whatman LK6D silica TLC plate. Chromatograms were developed in ethyl acetate:hexane (50:50, v/v). The products were visualized by autoradiography.

Crystallography. Crystals of ChOMT and IOMT were grown by vapor diffusion in hanging drops containing a 1:1 mixture of protein and crystallization buffer (ChOMT-12% (w/v) PEG 8000, 0.05 M HEPES (pH 7.5), 0.3 M ammonium acetate, 2 mM DTT at 4° C.; IOMT-17% (w/v) PEG 8000, 0.05 M Taps (pH 8.25), 0.35 M lithium sulfate, 2 mM DTT, 15° C.). Crystals for both proteins grew in space group C2 with one molecule per asymmetric unit. Unit cell dimensions for ChOMT were a=127.19 Å, b=53.79 Å, c=73.55 Å, β=125.55°. IOMT cell dimensions were a=145.56 Å, b=50.54 Å, c=63.82 Å, β=106.69°. Diffraction data was collected from single crystals mounted in a cryoloop and flash frozen in a nitrogen stream at 105 K. All diffraction data was collected at the Stanford Synchrotron Radiation Facility, beamline 9-2 (IOMT data and ChOMT Se-met data) on a Quantum 4 CCD detector and beamline 7-1 (ChOMT-isoliquiritigenin complex) on a 30 cm MAR imaging plate. All images were indexed and scaled using DENZO and the reflections merged with SCALEPACK. ChOMT and IOMT structures were determined using multiple wavelength anomalous dispersion (MAD) phasing on the Se-met substituted protein. Initial heavy atom sites were found with SOLVE. SHARP was used to refine the initial sites and to locate additional sites. MAD phases were improved with SOLOMON. Subsequent complexes were solved by the difference Fourier method. All refinements were carried out using CNS. During refinements, structure factors obtained from intensity data were used to generate SIGMAA-weighted |2F_(o)−F_(c)| and |F_(o)−F_(c)| electron density maps with phases calculated from the structure of the in-progress model. Inspection of the electron density maps and model building was performed in O. The quality of all models was assessed using the program PROCHECK. For the ChOMT-isoliquiritigenin complex 92.6%, 6.4%, 0.7%, and 0.3% of the residues were found in the most favored, the allowed, the generously allowed, and the disallowed regions of the Ramachandran plot, respectively, with a G factor of 0.39. For the IOMT-isoformononetin complex, 91%, 8%, and 1% of the residues were found in the most favored, the allowed, and the generously allowed regions of the Ramachandran plot, respectively, with a G factor of 0.30.

Recombinant proteins were expressed in E. coli as N-terminal polyhistidine tagged proteins and purified by Ni⁺² affinity chromatography and gel filtration. ChOMT and IOMT possess specific activities comparable to published values. Both ChOMT and IOMT were crystallized from polyethylene glycol (PEG) solutions in the presence of a two-fold molar excess of SAM or SAH. Structures of ChOMT and IOMT were determined with seleno-methionine (Se-met) substituted proteins using multiwavelength anomalous dispersion (MAD) phasing. Additional structures of substrate and product complexes were determined by molecular replacement based on the Se-met derived structures (FIG. 2A-D).

The present invention provides for the first time the x-ray crystal structures of ChOMT (Table 3) and IOMT (Table 4), two S-adenosyl-L-methionine (SAM) dependent OMTs from Medicago sativa L. ChOMT and IOMT are 40 kDa proteins and exist as homodimers in solution. These methyltransferases possess SAM binding domains that align structurally with previously characterized viral, bacterial, archaebacterial, and mammalian OMT's. The fold of the catalytic SAM binding domain is conserved throughout all classes of SAM-dependent methyltransferases. Unique features of plant O-methyltransferases include the presence of a second domain involved in dimerization and the contribution of the dimer interface to the substrate-binding site. The structures presented here complexed with substrates and products reveal a characteristic mechanism for methyl transfer by plant OMTs. Furthermore, these studies provide the first structural understanding of substrate discrimination displayed by the large family of plant OMTs.

TABLE 3 Crystallographic data, phasing, and refinement information for ChOMT λ₁ λ₂ λ₃ λ₄ Isoliquiritigenin Wavelength (Å) 0.9287 0.9795 0.9797 0.9793 1.03 Resolution range (Å)   99-2.00   99-2.00   99-2.00   99-2.00   99-1.82 Observations 97,770 103,406 74,366 53,106 94,322 Unique reflections¹ 49,336 49,023 48,231 40,256 32,685 Completeness¹ (%)   93 (81)   92 (61)   91 (55)   75 (49)   90 (48) I/σ¹ 21.6 (3.7) 22.4 (3.9) 20.0 (3.0) 17.3 (1.3) 25.6 (1.5) R_(sym) ^(1, 2) (%)   4.1 (20)  4.0 (14)  3.3 (15)  3.8 (46)  5.0 (66) No. Se sites 15 15 15 15 PPiso³ 2.4/1.7 3.0/2.2 0.53/0.43 (acentric/centric) PPano³ 2.2 2.9 2.0 1.9 R_(cryst) ⁴/R_(free) ⁵ (%) 23.6/27.8 21.4/25.9 Protein atoms 2620 2620 Water molecules 118 214 SAH atoms 26 26 Chalcone atoms 0 19 R.m.s. deviations Bonds (Å) 0.019 0.006 Angles (°) 1.9 1.2 Average B-factors Protein (Å²) 41.0 38.2 Water (Å²) 43.8 45.6 SAH (Å²) 44.0 35.4 Iso A/B⁶ (Å²) 29.8/41.7 ¹Number in parenthesis is for highest resolution shell. Unique reflections and coverage for λl, λ2, λ3, and λ4 assume that F⁺ is not equivalent to F⁻. ² R_(sym) = [I_(h) − <I_(h)>|/I_(h), where <I_(h)> is the average intensity over symmetry equivalent reflections; ³Phasing power = <|F_(H(calc))/|E|>, where F_(H(calc)) is the calculated difference and E is the lack of closure; ⁴R-factor = |F_(obs) − F_(calc)|/F_(obs), where summation is over the data used for refinement; ⁵R_(free)-factor was calculated using 5% of data excluded from refinement; ⁶A and B distinguish two observed alternative isoliquiritigenin (iso) conformations.

TABLE 4 Crystallographic data, phasing, and refinement information for IOMT Isoformono- λ₁ λ₂ λ₃ netin Wavelength (Å) 0.9746 0.9785 0.9787 0.9200 Resolution range   99-1.52   99-1.52   99-1.65   99-1.40 (Å) Observations 243,257 241,156 74,366 152,679 Unique 126,699 126,210 48,231 83,124 reflections¹ Completeness¹   96 (81)   95 (79)   91 (55)   94 (65) (%) I/σ¹ 15.6 (1.4) 15.2 (1.2) 16.7 (3.0) 19.1 (1.3) R_(sym) ^(1 ,2) (%)  3.7 (69)  4.0 (75)  3.5 (30)  4.0 (70) No. Se sites 8 8 8 PPiso³ 3.2/2.2 2.9/1.6 (acentric/centric) PPano³ 3.4 4.7 4.4 R_(cryst) ⁴/R_(free) ⁵ (%) 21.9/23.6 22.0/24.0 Protein atoms 2736 2736 Water molecules 143 308 SAH atoms 26 26 Isoformononetin 20 atoms R.m.s. deviations Bonds (Å) 0.022 0.020 Angles (°) 1.7 1.8 Average B-factors Protein (Å²) 22.3 19.4 Water (Å²) 31.2 25.5 SAH (Å²) 18.1 15.7 Isoformononetin 24.4 (Å²) ¹Number in parenthesis is for highest resolution shell. Unique reflections and coverage for λl, λ2, and λ3 assume that F⁺ is not equivalent to F⁻. ²R_(sym) = |I_(h) − <I_(h)>|/I_(h), where <I_(h)> is the average intensity over symmetry equivalent reflections; ³Phasing power = <|F_(H(calc))/|E|>, where F_(H(calc)) is the calculated difference and E is the lack of closure; ⁴R-factor = |F_(obs) − F_(calc)|/F_(obs), where summation is over the data used for refinement; ⁵R_(free)-factor was calculated using 5% of data excluded from refinement.

ChOMT (FIG. 3A-C) and IOMT (FIG. 4A-C) exhibit a common tertiary structure consisting of a large C-terminal catalytic domain responsible for SAM binding and substrate methylation and a smaller N-terminal domain involved in dimerization and formation of the back wall of the substrate binding site. Due to this conservation of fold, the RMSD for alignment of the catalytic domains is 1.4 Å, while both the catalytic and dimerization domains align with an RMSD of 1.8 Å for all backbone atoms. The catalytic domain contains a core α/β Rossmann fold common to nucleotide binding proteins. Structural alignments with representative DNA and small molecule methyltransferases illustrate the presence of a conserved fold involved in SAM/SAH binding (FIG. 5A). Unlike most structurally characterized methyltransferases that are monomeric, ChOMT and IOMT form homologous homodimers in their respective crystalline lattices. The monomers in both cases are related by a crystallographic two-fold axis. While ChOMT and IOMT were originally characterized as monomers, the recombinant proteins exhibit no monomer formation in solution. Dimerization appears to be critical for activity and most likely occurs in vivo as well as in vitro. In fact, the presence of a dimerization interface appears to be common to plant OMT's and intimately contribute to substrate binding.

In ChOMT, the extensive dimerization interface buries approximately 8990 Å² of surface area, encompassing 30% of the available surface area of the dimer (FIG. 3A). Met 29, Thr 32, and Thr 33 insert into the catalytic domain of the neighboring molecule thus forming the back wall of the neighboring molecule's active site. The extent of the IOMT interface is comparable with 8597 Å² of buried surface area at the interface, comprising approximately 30% of the available surface area of the dimer (FIG. 4A). Tyr 25, Phe 27, and Ile 28 form the back wall of the catalytic domain of the dyad related monomer.

SAM/SAH Binding

The structures of ChOMT and IOMT complexed with SAH clearly delineate a conserved SAH/SAM binding motif. The catalytic domains of ChOMT and IOMT maintain homologous α/β folds consisting of helices 9-13 and β-strands 3-9 (FIG. 5B). In addition to conservation of the OMT tertiary structure, positional conservation of the amino acids involved in cofactor binding is evident from the crystal structures of ChOMT and IOMT as well as sequence alignments of plant OMT's (FIG. 5B). SAH binding within the active site pocket of ChOMT is mediated through a network of hydrogen bonds as well as van der Waal's interactions (FIG. 3B). IOMT binds SAH through a similar set of interactions FIG. 4B). The residues involved in hydrogen bonding and van der Waal's interactions with SAM/SAH are spatially equivalent in both methyltransferases. The two structures of ChOMT and IOMT highlight the analogous orientation of the bound SAH as well as the common chemical features of the SAM/SAH binding motif.

Hydroxylated Substrate Binding

Because of the broad structural diversity of plant phenylpropanoid compounds, the majority of plant OMTs possess highly selective substrate and positional specificity. Efficient substrate discrimination and binding is achieved in ChOMT and IOMT through shape selectivity dictated by van der Waal's interactions including a rich set of aromatic and aliphatic side chains, and by specific hydrogen bonding patterns. In ChOMT, the isoliquiritigenin substrate adopts two conformations within the active site via an approximately 180° rotation around the carbonyl carbon, resulting in two distinct binding modes for the B-ring of isoliquiritigenin (FIG. 3B, C). The position of the A-ring, which presents the 2′-hydroxyl group to SAM for methylation, is conserved in both conformers. The A-ring is bound by the thioether moieties of Met 189 and Met 329. Thr 332 and the 4′-hydroxyl moiety of the substrate are within hydrogen bonding distance, which secures the substrate within the active site and most likely ensures that the A-ring 2′-hydroxyl is firmly positioned for deprotonation followed with methylation by the putative catalytic base, His 278, and the methyl donor, SAM, respectively. The back wall of the active site consists of residues Met 29, Thr 32, and Thr 33 donated from the partner monomer (FIG. 6A).

The IOMT active site uses the same chemical features for substrate binding as ChOMT. Due to the lack of aqueous stability exhibited by the isoflavanone substrate, 2,7,4′-trihydroxyisoflavanone, the isoflavone daidzein was substituted in crystallization experiments as IOMT exhibits considerable activity towards this compound. Co-crystallization of IOMT with SAM and daidzein resulted in the formation of a product complex consisting of SAH and isoformononetin (FIG. 4B, C). Met 168 and Met 311 constrain the A-ring and help position the 7-hydroxyl group for methylation. Given the high degree of conservation of both methionines in plant OMTs, the stereochemical features of these interactions are most likely conserved throughout the plant OMT superfamily (FIG. 5B). Furthermore, this degree of amino acid conservation suggests that the interaction of the methionine thioether group with hydroxylated phenyl groups plays a major energetic role in orienting the aromatic ring presenting a hydroxyl group to SAM and the OMT catalytic machinery.

Tyr 25, Phe 27, and Ile 28 of the dyad related monomer form the back wall of to the active site (FIG. 6B). While these residues are contributed from the symmetrically arranged monomer, they do not align sequentially with the equivalent residues in ChOMT. These contacts between the active site of one monomer and the side chains from the symmetrically arranged monomer have important repercussions for substrate specificity. In studies of OMTs involved in berberine biosynthesis, for example, high sequence conservation (93-99% identity) of four methyltransferases allowed the formation of heterodimers. Different substrate specificity profiles were seen in the different isoforms and in some cases heterodimer formation allowed for the acceptance of new substrates. Clearly, the dimer interface in plant OMTs can modulate the choice of chemically similar substrates through variation in the dimer interface.

In order to investigate the structural basis for the apparent physiological preference of IOMT for its putative in vivo substrate, 2,4′,7-trihydroxyisoflavanone, the four possible stereoisomers of 2,4′,7-trihydroxyisoflavanone were modeled in the IOMT active site. The resulting model suggests that the optimally binding isomer is (2S,3S)-2,4′,7-trihydroxyisoflavanone (FIG. 6B). All four stereoisomers were modeled by superimposing the 4′-hydroxyl moiety of the isoflavanone onto the observed location of the 7-methoxy group of isoformononetin. The resulting substrate specificity is most likely conferred by hydrogen bonding interactions which dictate the positioning of the physiological substrate, 2,4′,7-trihydroxyisoflavanone, near the reactive methyl group of SAM and the catalytic base, His 257. The additional hydroxyl group located at carbon 2 and the ether oxygen at position 1 of the C-ring form putative hydrogen bonds with the side chain carbonyl and side chain amide of Asn 310, respectively. In addition, the 2-hydroxyl moiety of the C-ring potentially forms an additional hydrogen bond with the side chain sulfhydryl group of Cys 313. In a chemically similar manner, the carbonyl oxygen at carbon 4 of the C-ring forms a putative hydrogen bond with Cys 117. All of these newly formed interactions are not seen in the isoformononetin complex and likely serve to specifically sequester the isoflavanone substrate (FIG. 6B).

The accretion of hydrogen bonding interactions and the preservation of aromatic and hydrophobic interactions around the bound isoflavanone suggests that IOMT might display an energetic preference for the isoflavanone intermediate rather then the dehydrated isoflavone, daidzein. Regardless of the substrate preference displayed in vitro, in vivo conditions most likely only allow for the presence of the isoflavanone substrate. In addition, in vivo analysis suggests that IOMT and IFS form a complex upon induction of the defense response, which would provide for efficient channeling of the isoflavanone product of IFS to IOMT.

Reaction Mechanism

Based both upon the structures of ChOMT and IOMT and sequence alignments with the large family of plant OMTs, methylation proceeds via base-assisted deprotonation of the hydroxyl group followed by a nucleophilic attack of the newly generated phenolate anion of the substrate on the reactive methyl group of SAM. In ChOMT, deprotonation of the 2′-hydroxyl group of the A-ring by His 278, sets up the subsequent attack by the hydroxyl anion on the methyl group of SAM. Because the sulfur of SAM is positively charged, the transmethylation process is easily facilitated by the deprotonation step. Glu 306 and Glu 337 bracket the catalytic histidine, with a hydrogen-bonding interaction of the Nδ nitrogen to the carboxylate group of Glu 337 (FIG. 2B). This interaction ensures the optimal orientation of the imidazole group for deprotonation of the 2′-hydroxyl of the isoliquiritigenin substrate by the Nδ nitrogen of His 278 (FIG. 6A). Mutations of His 278 to leucine, alanine, glutamine, lysine, and asparagine completely eliminated methyltransferase activity further implicating His 278 as an important catalytic residue (FIG. 7A).

Catalysis in IOMT proceeds through a comparable mechanism with His 257 serving as the base responsible for deprotonation of the 7-hydroxyl group on the A-ring of daidzein (FIG. 6B). Similarly to ChOMT, Asp 288 and Glu 318 sterically constrain His 257 and position the Nδ nitrogen through a hydrogen bond with Glu 318. This same catalytic mechanism would be predicted for the putative physiological substrate, 2,7,4′-trihydroxyisoflavanone. Mutations of His 257 to leucine, isoleucine, glutamine, and aspartate eliminated methyltransferase activity towards daidzein. Mutation of the active site histidine to lysine displayed greatly diminished activity compared to wild type enzyme (FIG. 7B).

Other methyltransferases follow similar SN₂ pathways involving oxygen, nitrogen, and carbon based nucleophiles. The addition of methyl groups to carbon, such as seen in the C5 methylation of cytosine, usually proceeds via initial attack of an active site cysteine on C6, generating a resonance-stabilized carbanion at C5. Small molecule O-methylation reactions, such as in catechol O-methyltransferase, are facilitated by metal-mediated deprotonation. Glycine N-methyltransferase and PvuII DNA-(cytosine N4) methyltransferase are postulated to use a glutamate residue to deprotonate the amino moiety thus facilitating methyl transfer. The putative role of histidine as a catalytic base has only been seen in one other structurally characterized methyltransferase, PRMT3 (protein arginine N-methyltransferase). The role of histidine in ChOMT and IOMT is similar to the reaction mechanism proposed for PRMT3, which utilizes a His-Asp proton relay system.

Materials. The pET-15b expression vector and E. coli strain BL21(DE3) were purchased from Novagen. Ni²⁺-NTA resin was purchased from Qiagen. Benzamidine Sepharose and Superdex 200 FPLC columns were obtained from Pharmacia. Se-met, thrombin, S-adenosyl-L-methionine, and S-adenosyl-L-homocysteine were obtained from Sigma. All oligonucleotides were purchased from Operon, Inc. Adenosyl-L-methionine-S-(methyl-¹⁴C) was purchased from New England Nuclear (NEN). 2′,4,4′-trihydroxychalcone and 4′,7-dihydroxyisofiavone were acquired from Indofine.

Coordinates. Coordinates have been deposited in the Protein Data Bank (accession codes 1FPQ, 1FP1, 1FPX, 1FP2 for the ChOMT-SAH, ChOMT-SAH-isoliquiritigenin, IOMT-SAH, and IOMT-SAH-isoformononetin complexes, respectively). Access to the foregoing information in the Protein Data Bank can be found at www.rcsb.org.

While the foregoing has been presented with reference to particular embodiments of the invention, it will be appreciated by those skilled in the art that changes in these embodiments may be made without departing from the principles and spirit of the invention, the scope of which is defined by the appended claims.

APPENDIX A ATOM TYPE RES # X Y Z OCC B ATOM ATOM N N THR A 20 . 27.563 8.007 33.594 1.00 37.27 . 1 1 ATOM C CA THR A 20 . 26.478 7.573 32.653 1.00 37.30 . 1 2 ATOM C C THR A 20 . 26.196 6.077 32.778 1.00 35.88 . 1 3 ATOM O O THR A 20 . 27.117 5.264 32.808 1.00 35.00 . 1 4 ATOM C CB THR A 20 . 26.862 7.891 31.179 1.00 38.58 . 1 5 ATOM O OG1 THR A 20 . 26.425 9.218 30.839 1.00 41.40 . 1 6 ATOM C CG2 THR A 20 . 26.249 6.899 30.225 1.00 39.42 . 1 7 ATOM N N GLU A 21 . 24.918 5.724 32.849 1.00 34.74 . 1 8 ATOM C CA GLU A 21 . 24.508 4.328 32.959 1.00 33.46 . 1 9 ATOM C C GLU A 21 . 24.938 3.563 31.702 1.00 32.65 . 1 10 ATOM O O GLU A 21 . 25.430 2.441 31.806 1.00 32.47 . 1 11 ATOM C CB GLU A 21 . 22.987 4.240 33.153 1.00 33.66 . 1 12 ATOM C CG GLU A 21 . 22.475 2.937 33.788 1.00 34.20 . 1 13 ATOM C CD GLU A 21 . 23.085 2.643 35.163 1.00 34.93 . 1 14 ATOM O OE1 GLU A 21 . 24.089 1.907 35.226 1.00 34.78 . 1 15 ATOM O OE2 GLU A 21 . 22.569 3.147 36.183 1.00 35.16 . 1 16 ATOM N N ASP A 22 . 24.768 4.166 30.521 1.00 31.28 . 1 17 ATOM C CA ASP A 22 . 25.178 3.504 29.272 1.00 30.50 . 1 18 ATOM C C ASP A 22 . 26.667 3.153 29.308 1.00 29.02 . 1 19 ATOM O O ASP A 22 . 27.064 2.072 28.873 1.00 28.09 . 1 20 ATOM C CB ASP A 22 . 24.903 4.387 28.040 1.00 31.76 . 1 21 ATOM C CG ASP A 22 . 23.444 4.335 27.581 1.00 34.44 . 1 22 ATOM O OD1 ASP A 22 . 22.906 3.220 27.357 1.00 34.38 . 1 23 ATOM O OD2 ASP A 22 . 22.830 5.417 27.424 1.00 34.57 . 1 24 ATOM N N SER A 23 . 27.488 4.076 29.813 1.00 27.66 . 1 25 ATOM C CA SER A 23 . 28.932 3.868 29.929 1.00 27.35 . 1 26 ATOM C C SER A 23 . 29.285 2.790 30.950 1.00 25.96 . 1 27 ATOM O O SER A 23 . 30.168 1.960 30.719 1.00 25.43 . 1 28 ATOM C CB SER A 23 . 29.638 5.169 30.350 1.00 28.92 . 1 29 ATOM O OG SER A 23 . 30.027 5.928 29.223 1.00 32.57 . 1 30 ATOM N N ALA A 24 . 28.608 2.823 32.089 1.00 25.30 . 1 31 ATOM C CA ALA A 24 . 28.864 1.851 33.145 1.00 25.82 . 1 32 ATOM C C ALA A 24 . 28.556 0.428 32.675 1.00 26.27 . 1 33 ATOM O O ALA A 24 . 29.329 −0.488 32.938 1.00 26.40 . 1 34 ATOM C CB ALA A 24 . 28.041 2.181 34.371 1.00 24.04 . 1 35 ATOM N N CYS A 25 . 27.429 0.244 31.995 1.00 25.61 . 1 36 ATOM C CA CYS A 25 . 27.068 −1.084 31.509 1.00 26.57 . 1 37 ATOM C C CYS A 25 . 28.078 −1.540 30.462 1.00 26.48 . 1 38 ATOM O O CYS A 25 . 28.490 −2.705 30.458 1.00 26.51 . 1 39 ATOM C CB CYS A 25 . 25.656 −1.089 30.920 1.00 26.93 . 1 40 ATOM S SG CYS A 25 . 25.041 −2.755 30.525 1.00 29.22 . 1 41 ATOM N N LEU A 26 . 28.491 −0.626 29.586 1.00 25.97 . 1 42 ATOM C CA LEU A 26 . 29.486 −0.950 28.563 1.00 26.13 . 1 43 ATOM C C LEU A 26 . 30.775 −1.458 29.207 1.00 25.87 . 1 44 ATOM O O LEU A 26 . 31.393 −2.395 28.712 1.00 25.05 . 1 45 ATOM C CB LEU A 26 . 29.804 0.276 27.685 1.00 27.27 . 1 46 ATOM C CG LEU A 26 . 30.941 0.084 26.673 1.00 28.28 . 1 47 ATOM C CD1 LEU A 26 . 30.590 −1.045 25.705 1.00 29.12 . 1 48 ATOM C CD2 LEU A 26 . 31.177 1.387 25.892 1.00 29.00 . 1 49 ATOM N N SER A 27 . 31.193 −0.826 30.300 1.00 25.88 . 1 50 ATOM C CA SER A 27 . 32.403 −1.254 31.003 1.00 25.52 . 1 51 ATOM C C SER A 27 . 32.173 −2.615 31.629 1.00 24.43 . 1 52 ATOM O O SER A 27 . 33.056 −3.473 31.636 1.00 25.07 . 1 53 ATOM C CB SER A 27 . 32.776 −0.255 32.102 1.00 25.69 . 1 54 ATOM O OG SER A 27 . 33.366 0.891 31.537 1.00 27.54 . 1 55 ATOM N N ALA A 28 . 30.985 −2.808 32.173 1.00 23.85 . 1 56 ATOM C CA ALA A 28 . 30.671 −4.085 32.778 1.00 24.35 . 1 57 ATOM C C ALA A 28 . 30.722 −5.171 31.702 1.00 24.40 . 1 58 ATOM O O ALA A 28 . 31.185 −6.282 31.960 1.00 25.61 . 1 59 ATOM C CB ALA A 28 . 29.310 −4.032 33.409 1.00 23.05 . 1 60 HETA N N MSE A 29 . 30.267 −4.846 30.490 1.00 24.81 . 1 61 HETA C CA MSE A 29 . 30.277 −5.821 29.393 1.00 24.21 . 1 62 HETA C C MSE A 29 . 31.701 −6.120 28.949 1.00 24.16 . 1 63 HETA O O MSE A 29 . 32.011 −7.254 28.595 1.00 24.97 . 1 64 HETA C CB MSE A 29 . 29.435 −5.336 28.205 1.00 23.78 . 1 65 HETA C CG MSE A 29 . 27.920 −5.345 28.447 1.00 24.63 . 1 66 HETA SE SE MSE A 29 . 26.917 −4.615 27.061 1.00 19.25 . 1 67 HETA C CE MSE A 29 . 27.279 −2.891 27.327 1.00 25.20 . 1 68 ATOM N N VAL A 30 . 32.572 −5.115 28.962 1.00 23.98 . 1 69 ATOM C CA VAL A 30 . 33.965 −5.323 28.598 1.00 24.50 . 1 70 ATOM C C VAL A 30 . 34.610 −6.191 29.702 1.00 26.35 . 1 71 ATOM O O VAL A 30 . 35.442 −7.079 29.432 1.00 26.02 . 1 72 ATOM C CB VAL A 30 . 34.724 −3.970 28.500 1.00 25.00 . 1 73 ATOM C CG1 VAL A 30 . 36.167 −4.213 28.108 1.00 25.56 . 1 74 ATOM C CG2 VAL A 30 . 34.040 −3.041 27.471 1.00 24.84 . 1 75 ATOM N N LEU A 31 . 34.221 −5.920 30.946 1.00 26.98 . 1 76 ATOM C CA LEU A 31 . 34.718 −6.662 32.110 1.00 29.12 . 1 77 ATOM C C LEU A 31 . 34.383 −8.151 32.087 1.00 29.12 . 1 78 ATOM O O LEU A 31 . 35.238 −9.003 32.313 1.00 30.24 . 1 79 ATOM C CB LEU A 31 . 34.110 −6.090 33.389 1.00 30.14 . 1 80 ATOM C CG LEU A 31 . 34.141 −6.995 34.627 1.00 31.59 . 1 81 ATOM C CD1 LEU A 31 . 35.587 −7.330 34.985 1.00 33.03 . 1 82 ATOM C CD2 LEU A 31 . 33.442 −6.307 35.790 1.00 31.13 . 1 83 ATOM N N THR A 32 . 33.122 −8.452 31.830 1.00 29.62 . 1 84 ATOM C CA THR A 32 . 32.662 −9.825 31.838 1.00 29.41 . 1 85 ATOM C C THR A 32 . 33.101 −10.699 30.673 1.00 29.54 . 1 86 ATOM O O THR A 32 . 32.994 −11.926 30.752 1.00 28.32 . 1 87 ATOM C CB THR A 32 . 31.138 −9.868 31.977 1.00 29.85 . 1 88 ATOM O OG1 THR A 32 . 30.534 −9.017 30.994 1.00 30.45 . 1 89 ATOM C CG2 THR A 32 . 30.737 −9.394 33.367 1.00 28.66 . 1 90 ATOM N N THR A 33 . 33.612 −10.081 29.610 1.00 28.93 . 1 91 ATOM C CA THR A 33 . 34.073 −10.826 28.443 1.00 28.90 . 1 92 ATOM C C THR A 33 . 35.594 −10.772 28.338 1.00 29.04 . 1 93 ATOM O O THR A 33 . 36.167 −11.155 27.321 1.00 29.45 . 1 94 ATOM C CB THR A 33 . 33.452 −10.262 27.130 1.00 29.35 . 1 95 ATOM O OG1 THR A 33 . 33.843 −8.897 26.953 1.00 29.12 . 1 96 ATOM C CG2 THR A 33 . 31.942 −10.323 27.187 1.00 28.84 . 1 97 ATOM N N ASN A 34 . 36.238 −10.315 29.408 1.00 30.02 . 1 98 ATOM C CA ASN A 34 . 37.699 −10.173 29.489 1.00 30.62 . 1 99 ATOM C C ASN A 34 . 38.576 −11.369 29.076 1.00 29.56 . 1 100 ATOM O O ASN A 34 . 39.762 −11.203 28.773 1.00 28.38 . 1 101 ATOM C CB ASN A 34 . 38.098 −9.730 30.917 1.00 32.96 . 1 102 ATOM C CG ASN A 34 . 37.527 −10.638 32.021 1.00 35.68 . 1 103 ATOM O OD1 ASN A 34 . 38.020 −10.639 33.147 1.00 38.22 . 1 104 ATOM N ND2 ASN A 34 . 36.477 −11.384 31.709 1.00 37.23 . 1 105 ATOM N N LEU A 35 . 38.008 −12.568 29.037 1.00 28.16 . 1 106 ATOM C CA LEU A 35 . 38.797 −13.746 28.682 1.00 27.20 . 1 107 ATOM C C LEU A 35 . 39.198 −13.821 27.199 1.00 26.44 . 1 108 ATOM O O LEU A 35 . 40.224 −14.401 26.850 1.00 25.73 . 1 109 ATOM C CB LEU A 35 . 38.018 −15.005 29.088 1.00 28.48 . 1 110 ATOM C CG LEU A 35 . 38.725 −16.358 28.992 1.00 29.33 . 1 111 ATOM C CD1 LEU A 35 . 39.971 −16.358 29.856 1.00 29.23 . 1 112 ATOM C CD2 LEU A 35 . 37.741 −17.450 29.438 1.00 29.48 . 1 113 ATOM N N VAL A 36 . 38.409 −13.216 26.322 1.00 26.14 . 1 114 ATOM C CA VAL A 36 . 38.710 −13.254 24.894 1.00 26.17 . 1 115 ATOM C C VAL A 36 . 40.027 −12.579 24.540 1.00 26.45 . 1 116 ATOM O O VAL A 36 . 40.734 −13.009 23.631 1.00 25.87 . 1 117 ATOM C CB VAL A 36 . 37.571 −12.603 24.062 1.00 25.56 . 1 118 ATOM C CG1 VAL A 36 . 37.898 −12.677 22.570 1.00 25.46 . 1 119 ATOM C CG2 VAL A 36 . 36.262 −13.309 24.338 1.00 25.42 . 1 120 ATOM N N TYR A 37 . 40.372 −11.529 25.276 1.00 26.84 . 1 121 ATOM C CA TYR A 37 . 41.597 −10.780 25.015 1.00 27.06 . 1 122 ATOM C C TYR A 37 . 42.860 −11.646 25.097 1.00 26.64 . 1 123 ATOM O O TYR A 37 . 43.664 −11.674 24.164 1.00 24.83 . 1 124 ATOM C CB TYR A 37 . 41.657 −9.594 25.996 1.00 31.23 . 1 125 ATOM C CG TYR A 37 . 42.764 −8.587 25.779 1.00 33.94 . 1 126 ATOM C CD1 TYR A 37 . 43.093 −7.690 26.791 1.00 36.05 . 1 127 ATOM C CD2 TYR A 37 . 43.477 −8.521 24.582 1.00 36.05 . 1 128 ATOM C CE1 TYR A 37 . 44.103 −6.752 26.627 1.00 38.01 . 1 129 ATOM C CE2 TYR A 37 . 44.503 −7.580 24.406 1.00 37.53 . 1 130 ATOM C CZ TYR A 37 . 44.804 −6.700 25.441 1.00 38.43 . 1 131 ATOM O OH TYR A 37 . 45.801 −5.753 25.315 1.00 41.15 . 1 132 ATOM N N PRO A 38 . 43.065 −12.369 26.218 1.00 26.85 . 1 133 ATOM C CA PRO A 38 . 44.267 −13.196 26.291 1.00 27.01 . 1 134 ATOM C C PRO A 38 . 44.278 −14.334 25.268 1.00 26.53 . 1 135 ATOM O O PRO A 38 . 45.336 −14.718 24.784 1.00 26.33 . 1 136 ATOM C CB PRO A 38 . 44.266 −13.686 27.741 1.00 27.31 . 1 137 ATOM C CG PRO A 38 . 42.835 −13.602 28.147 1.00 27.56 . 1 138 ATOM C CD PRO A 38 . 42.400 −12.312 27.528 1.00 27.60 . 1 139 ATOM N N ALA A 39 . 43.102 −14.864 24.941 1.00 26.90 . 1 140 ATOM C CA ALA A 39 . 42.999 −15.934 23.942 1.00 26.71 . 1 141 ATOM C C ALA A 39 . 43.498 −15.421 22.589 1.00 25.98 . 1 142 ATOM O O ALA A 39 . 44.261 −16.095 21.891 1.00 26.72 . 1 143 ATOM C CB ALA A 39 . 41.550 −16.398 23.823 1.00 27.06 . 1 144 ATOM N N VAL A 40 . 43.061 −14.223 22.214 1.00 25.83 . 1 145 ATOM C CA VAL A 40 . 43.478 −13.625 20.951 1.00 24.63 . 1 146 ATOM C C VAL A 40 . 44.949 −13.270 20.981 1.00 24.74 . 1 147 ATOM O O VAL A 40 . 45.675 −13.536 20.021 1.00 24.91 . 1 148 ATOM C CB VAL A 40 . 42.656 −12.348 20.633 1.00 25.09 . 1 149 ATOM C CG1 VAL A 40 . 43.252 −11.614 19.436 1.00 25.00 . 1 150 ATOM C CG2 VAL A 40 . 41.214 −12.727 20.367 1.00 24.17 . 1 151 ATOM N N LEU A 41 . 45.405 −12.662 22.074 1.00 24.91 . 1 152 ATOM C CA LEU A 41 . 46.818 −12.307 22.173 1.00 24.03 . 1 153 ATOM C C LEU A 41 . 47.689 −13.561 22.069 1.00 23.62 . 1 154 ATOM O O LEU A 41 . 48.685 −13.574 21.354 1.00 22.69 . 1 155 ATOM C CB LEU A 41 . 47.114 −11.605 23.503 1.00 24.68 . 1 156 ATOM C CG LEU A 41 . 48.597 −11.381 23.805 1.00 24.18 . 1 157 ATOM C CD1 LEU A 41 . 49.193 −10.427 22.800 1.00 25.97 . 1 158 ATOM C CD2 LEU A 41 . 48.762 −10.821 25.233 1.00 24.87 . 1 159 ATOM N N ASN A 42 . 47.307 −14.603 22.799 1.00 24.79 . 1 160 ATOM C CA ASN A 42 . 48.039 −15.872 22.807 1.00 26.14 . 1 161 ATOM C C ASN A 42 . 48.150 −16.445 21.397 1.00 26.36 . 1 162 ATOM O O ASN A 42 . 49.182 −17.008 21.019 1.00 27.51 . 1 163 ATOM C CB ASN A 42 . 47.316 −16.877 23.717 1.00 26.92 . 1 164 ATOM C CG ASN A 42 . 48.061 −18.200 23.852 1.00 28.53 . 1 165 ATOM O OD1 ASN A 42 . 49.263 −18.231 24.102 1.00 28.57 . 1 166 ATOM N ND2 ASN A 42 . 47.336 −19.300 23.702 1.00 29.95 . 1 167 ATOM N N ALA A 43 . 47.082 −16.301 20.623 1.00 27.08 . 1 168 ATOM C CA ALA A 43 . 47.063 −16.813 19.252 1.00 27.51 . 1 169 ATOM C C ALA A 43 . 47.949 −15.956 18.355 1.00 27.53 . 1 170 ATOM O O ALA A 43 . 48.686 −16.474 17.517 1.00 27.36 . 1 171 ATOM C CB ALA A 43 . 45.639 −16.839 18.734 1.00 26.67 . 1 172 ATOM N N ALA A 44 . 47.876 −14.639 18.540 1.00 28.02 . 1 173 ATOM C CA ALA A 44 . 48.688 −13.709 17.769 1.00 28.14 . 1 174 ATOM C C ALA A 44 . 50.174 −14.020 17.946 1.00 28.65 . 1 175 ATOM O O ALA A 44 . 50.949 −13.983 16.988 1.00 28.17 . 1 176 ATOM C CB ALA A 44 . 48.399 −12.287 18.215 1.00 29.37 . 1 177 ATOM N N ILE A 45 . 50.566 −14.316 19.185 1.00 28.53 . 1 178 ATOM C CA ILE A 45 . 51.950 −14.640 19.511 1.00 29.10 . 1 179 ATOM C C ILE A 45 . 52.395 −15.950 18.851 1.00 30.03 . 1 180 ATOM O O ILE A 45 . 53.488 −16.035 18.289 1.00 29.74 . 1 181 ATOM C CB ILE A 45 . 52.136 −14.765 21.050 1.00 28.46 . 1 182 ATOM C CG1 ILE A 45 . 51.976 −13.387 21.712 1.00 28.48 . 1 183 ATOM C CG2 ILE A 45 . 53.496 −15.349 21.369 1.00 28.86 . 1 184 ATOM C CD1 ILE A 45 . 51.752 −13.451 23.213 1.00 28.75 . 1 185 ATOM N N ASP A 46 . 51.554 −16.974 18.922 1.00 31.70 . 1 186 ATOM C CA ASP A 46 . 51.904 −18.260 18.324 1.00 33.50 . 1 187 ATOM C C ASP A 46 . 51.983 −18.158 16.794 1.00 33.77 . 1 188 ATOM O O ASP A 46 . 52.781 −18.845 16.162 1.00 34.47 . 1 189 ATOM C CB ASP A 46 . 50.896 −19.331 18.739 1.00 35.38 . 1 190 ATOM C CG ASP A 46 . 50.803 −19.492 20.243 1.00 38.10 . 1 191 ATOM O OD1 ASP A 46 . 51.858 −19.496 20.926 1.00 39.82 . 1 192 ATOM O OD2 ASP A 46 . 49.666 −19.628 20.747 1.00 40.65 . 1 193 ATOM N N LEU A 47 . 51.161 −17.294 16.209 1.00 33.49 . 1 194 ATOM C CA LEU A 47 . 51.167 −17.078 14.761 1.00 33.59 . 1 195 ATOM C C LEU A 47 . 52.265 −16.092 14.360 1.00 33.24 . 1 196 ATOM O O LEU A 47 . 52.404 −15.754 13.184 1.00 33.44 . 1 197 ATOM C CB LEU A 47 . 49.813 −16.536 14.295 1.00 33.17 . 1 198 ATOM C CG LEU A 47 . 48.633 −17.508 14.333 1.00 33.79 . 1 199 ATOM C CD1 LEU A 47 . 47.344 −16.753 14.078 1.00 33.76 . 1 200 ATOM C CD2 LEU A 47 . 48.837 −18.602 13.289 1.00 34.32 . 1 201 ATOM N N ASN A 48 . 53.033 −15.632 15.347 1.00 32.88 . 1 202 ATOM C CA ASN A 48 . 54.131 −14.681 15.139 1.00 33.12 . 1 203 ATOM C C ASN A 48 . 53.699 −13.418 14.397 1.00 32.04 . 1 204 ATOM O O ASN A 48 . 54.463 −12.887 13.600 1.00 32.51 . 1 205 ATOM C CB ASN A 48 . 55.279 −15.327 14.344 1.00 35.20 . 1 206 ATOM C CG ASN A 48 . 55.617 −16.731 14.824 1.00 37.65 . 1 207 ATOM O OD1 ASN A 48 . 55.106 −17.729 14.292 1.00 39.07 . 1 208 ATOM N ND2 ASN A 48 . 56.477 −16.818 15.836 1.00 37.66 . 1 209 ATOM N N LEU A 49 . 52.494 −12.927 14.660 1.00 31.57 . 1 210 ATOM C CA LEU A 49 . 52.003 −11.732 13.963 1.00 32.09 . 1 211 ATOM C C LEU A 49 . 52.792 −10.452 14.228 1.00 31.95 . 1 212 ATOM O O LEU A 49 . 52.968 −9.628 13.330 1.00 32.29 . 1 213 ATOM C CB LEU A 49 . 50.531 −11.484 14.299 1.00 31.91 . 1 214 ATOM C CG LEU A 49 . 49.564 −12.629 13.994 1.00 32.83 . 1 215 ATOM C CD1 LEU A 49 . 48.149 −12.126 14.133 1.00 32.07 . 1 216 ATOM C CD2 LEU A 49 . 49.808 −13.163 12.580 1.00 33.36 . 1 217 ATOM N N PHE A 50 . 53.260 −10.284 15.461 1.00 30.70 . 1 218 ATOM C CA PHE A 50 . 54.005 −9.090 15.835 1.00 30.40 . 1 219 ATOM C C PHE A 50 . 55.360 −9.031 15.155 1.00 30.42 . 1 220 ATOM O O PHE A 50 . 55.777 −7.974 14.672 1.00 30.29 . 1 221 ATOM C CB PHE A 50 . 54.146 −9.045 17.361 1.00 28.83 . 1 222 ATOM C CG PHE A 50 . 52.843 −9.177 18.069 1.00 27.46 . 1 223 ATOM C CD1 PHE A 50 . 52.504 −10.352 18.718 1.00 26.82 . 1 224 ATOM C CD2 PHE A 50 . 51.907 −8.147 18.013 1.00 27.40 . 1 225 ATOM C CE1 PHE A 50 . 51.242 −10.507 19.299 1.00 27.20 . 1 226 ATOM C CE2 PHE A 50 . 50.647 −8.294 18.590 1.00 26.96 . 1 227 ATOM C CZ PHE A 50 . 50.314 −9.476 19.231 1.00 27.05 . 1 228 ATOM N N GLU A 51 . 56.049 −10.168 15.119 1.00 31.24 . 1 229 ATOM C CA GLU A 51 . 57.352 −10.243 14.478 1.00 32.85 . 1 230 ATOM C C GLU A 51 . 57.168 −9.966 12.981 1.00 33.06 . 1 231 ATOM O O GLU A 51 . 57.970 −9.263 12.359 1.00 32.40 . 1 232 ATOM C CB GLU A 51 . 57.965 −11.635 14.696 1.00 34.38 . 1 233 ATOM C CG GLU A 51 . 59.444 −11.726 14.322 1.00 37.33 . 1 234 ATOM C CD GLU A 51 . 60.026 −13.117 14.526 1.00 38.96 . 1 235 ATOM O OE1 GLU A 51 . 59.703 −13.765 15.549 1.00 41.32 . 1 236 ATOM O OE2 GLU A 51 . 60.822 −13.560 13.671 1.00 40.20 . 1 237 ATOM N N ILE A 52 . 56.097 −10.510 12.411 1.00 33.22 . 1 238 ATOM C CA ILE A 52 . 55.802 −10.305 10.997 1.00 33.30 . 1 239 ATOM C C ILE A 52 . 55.634 −8.825 10.715 1.00 33.62 . 1 240 ATOM O O ILE A 52 . 56.260 −8.285 9.816 1.00 33.72 . 1 241 ATOM C CB ILE A 52 . 54.520 −11.063 10.581 1.00 33.59 . 1 242 ATOM C CG1 ILE A 52 . 54.814 −12.567 10.556 1.00 33.57 . 1 243 ATOM C CG2 ILE A 52 . 54.021 −10.574 9.221 1.00 32.58 . 1 244 ATOM C CD1 ILE A 52 . 53.589 −13.437 10.319 1.00 33.84 . 1 245 ATOM N N ILE A 53 . 54.793 −8.154 11.484 1.00 34.08 . 1 246 ATOM C CA ILE A 53 . 54.604 −6.732 11.268 1.00 35.05 . 1 247 ATOM C C ILE A 53 . 55.930 −5.981 11.472 1.00 35.93 . 1 248 ATOM O O ILE A 53 . 56.240 −5.041 10.738 1.00 34.82 . 1 249 ATOM C CB ILE A 53 . 53.517 −6.182 12.216 1.00 34.98 . 1 250 ATOM C CG1 ILE A 53 . 52.181 −6.861 11.899 1.00 34.65 . 1 251 ATOM C CG2 ILE A 53 . 53.392 −4.673 12.063 1.00 34.42 . 1 252 ATOM C CD1 ILE A 53 . 51.060 −6.564 12.884 1.00 34.81 . 1 253 ATOM N N ALA A 54 . 56.723 −6.416 12.450 1.00 37.32 . 1 254 ATOM C CA ALA A 54 . 58.008 −5.778 12.730 1.00 39.03 . 1 255 ATOM C C ALA A 54 . 58.997 −5.923 11.572 1.00 40.29 . 1 256 ATOM O O ALA A 54 . 59.980 −5.192 11.496 1.00 40.52 . 1 257 ATOM C CB ALA A 54 . 58.619 −6.356 14.004 1.00 39.01 . 1 258 ATOM N N LYS A 55 . 58.734 −6.858 10.667 1.00 42.13 . 1 259 ATOM C CA LYS A 55 . 59.621 −7.073 9.528 1.00 44.18 . 1 260 ATOM C C LYS A 55 . 59.113 −6.502 8.198 1.00 45.36 . 1 261 ATOM O O LYS A 55 . 59.543 −6.940 7.131 1.00 44.93 . 1 262 ATOM C CB LYS A 55 . 59.912 −8.570 9.377 1.00 45.05 . 1 263 ATOM C CG LYS A 55 . 60.808 −9.120 10.469 1.00 46.76 . 1 264 ATOM C CD LYS A 55 . 60.947 −10.624 10.376 1.00 47.88 . 1 265 ATOM C CE LYS A 55 . 61.921 −11.150 11.423 1.00 48.91 . 1 266 ATOM N NZ LYS A 55 . 62.045 −12.642 11.394 1.00 49.85 . 1 267 ATOM N N ALA A 56 . 58.210 −5.524 8.262 1.00 46.54 . 1 268 ATOM C CA ALA A 56 . 57.672 −4.898 7.052 1.00 48.29 . 1 269 ATOM C C ALA A 56 . 58.841 −4.341 6.247 1.00 49.61 . 1 270 ATOM O O ALA A 56 . 59.716 −3.687 6.815 1.00 49.75 . 1 271 ATOM C CB ALA A 56 . 56.711 −3.786 7.427 1.00 47.67 . 1 272 ATOM N N THR A 57 . 58.853 −4.589 4.934 1.00 51.25 . 1 273 ATOM C CA THR A 57 . 59.954 −4.140 4.078 1.00 52.70 . 1 274 ATOM C C THR A 57 . 60.522 −2.767 4.437 1.00 53.11 . 1 275 ATOM O O THR A 57 . 61.695 −2.674 4.810 1.00 53.98 . 1 276 ATOM C CB THR A 57 . 59.590 −4.217 2.566 1.00 53.62 . 1 277 ATOM O OG1 THR A 57 . 60.377 −3.270 1.835 1.00 55.00 . 1 278 ATOM C CG2 THR A 57 . 58.114 −3.974 2.334 1.00 54.18 . 1 279 ATOM N N PRO A 58 . 59.737 −1.679 4.316 1.00 53.04 . 1 280 ATOM C CA PRO A 58 . 60.426 −0.450 4.718 1.00 52.66 . 1 281 ATOM C C PRO A 58 . 60.363 −0.461 6.243 1.00 52.33 . 1 282 ATOM O O PRO A 58 . 59.406 −0.983 6.817 1.00 52.42 . 1 283 ATOM C CB PRO A 58 . 59.553 0.660 4.124 1.00 52.76 . 1 284 ATOM C CG PRO A 58 . 58.800 −0.025 3.018 1.00 52.84 . 1 285 ATOM C CD PRO A 58 . 58.476 −1.361 3.627 1.00 52.89 . 1 286 ATOM N N PRO A 59 . 61.377 0.093 6.922 1.00 51.73 . 1 287 ATOM C CA PRO A 59 . 61.325 0.086 8.387 1.00 51.03 . 1 288 ATOM C C PRO A 59 . 60.166 0.917 8.934 1.00 50.04 . 1 289 ATOM O O PRO A 59 . 60.025 2.097 8.604 1.00 50.03 . 1 290 ATOM C CB PRO A 59 . 62.690 0.651 8.780 1.00 51.48 . 1 291 ATOM C CG PRO A 59 . 63.008 1.583 7.640 1.00 51.60 . 1 292 ATOM C CD PRO A 59 . 62.595 0.766 6.436 1.00 51.73 . 1 293 ATOM N N GLY A 60 . 59.327 0.294 9.757 1.00 48.56 . 1 294 ATOM C CA GLY A 60 . 58.203 1.008 10.342 1.00 46.83 . 1 295 ATOM C C GLY A 60 . 56.952 1.065 9.486 1.00 45.57 . 1 296 ATOM O O GLY A 60 . 55.912 1.548 9.930 1.00 45.24 . 1 297 ATOM N N ALA A 61 . 57.047 0.573 8.256 1.00 44.41 . 1 298 ATOM C CA ALA A 61 . 55.912 0.575 7.341 1.00 43.30 . 1 299 ATOM C C ALA A 61 . 54.752 −0.276 7.860 1.00 42.63 . 1 300 ATOM O O ALA A 61 . 54.962 −1.327 8.461 1.00 42.27 . 1 301 ATOM C CB ALA A 61 . 56.353 0.069 5.979 1.00 43.05 . 1 302 ATOM N N PHE A 62 . 53.528 0.186 7.627 1.00 41.87 . 1 303 ATOM C CA PHE A 62 . 52.347 −0.549 8.057 1.00 41.29 . 1 304 ATOM C C PHE A 62 . 52.090 −1.704 7.098 1.00 40.34 . 1 305 ATOM O O PHE A 62 . 52.608 −1.715 5.982 1.00 40.06 . 1 306 ATOM C CB PHE A 62 . 51.123 0.369 8.109 1.00 42.61 . 1 307 ATOM C CG PHE A 62 . 51.125 1.319 9.276 1.00 43.61 . 1 308 ATOM C CD1 PHE A 62 . 49.932 1.662 9.907 1.00 44.82 . 1 309 ATOM C CD2 PHE A 62 . 52.313 1.874 9.745 1.00 44.24 . 1 310 ATOM C CE1 PHE A 62 . 49.921 2.546 10.993 1.00 45.84 . 1 311 ATOM C CE2 PHE A 62 . 52.318 2.758 10.825 1.00 44.60 . 1 312 ATOM C CZ PHE A 62 . 51.121 3.096 11.451 1.00 44.72 . 1 313 HETA N N MSE A 63 . 51.299 −2.677 7.542 1.00 38.69 . 1 314 HETA C CA MSE A 63 . 50.981 −3.847 6.727 1.00 36.83 . 1 315 HETA C C MSE A 63 . 49.484 −4.165 6.781 1.00 36.45 . 1 316 HETA O O MSE A 63 . 48.850 −4.021 7.830 1.00 35.59 . 1 317 HETA C CB MSE A 63 . 51.774 −5.068 7.225 1.00 36.26 . 1 318 HETA C CG MSE A 63 . 53.212 −5.181 6.707 1.00 36.10 . 1 319 HETA SE SE MSE A 63 . 54.150 −6.539 7.468 1.00 34.65 . 1 320 HETA C CE MSE A 63 . 53.449 −7.951 6.700 1.00 36.21 . 1 321 ATOM N N SER A 64 . 48.922 −4.590 5.648 1.00 35.09 . 1 322 ATOM C CA SER A 64 . 47.508 −4.951 5.581 1.00 34.37 . 1 323 ATOM C C SER A 64 . 47.389 −6.417 5.980 1.00 33.85 . 1 324 ATOM O O SER A 64 . 48.380 −7.143 5.996 1.00 33.81 . 1 325 ATOM C CB SER A 64 . 46.970 −4.782 4.155 1.00 34.35 . 1 326 ATOM O OG SER A 64 . 47.475 −5.805 3.315 1.00 33.94 . 1 327 ATOM N N PRO A 65 . 46.176 −6.872 6.319 1.00 34.20 . 1 328 ATOM C CA PRO A 65 . 45.973 −8.271 6.709 1.00 34.39 . 1 329 ATOM C C PRO A 65 . 46.438 −9.252 5.633 1.00 34.68 . 1 330 ATOM O O PRO A 65 . 46.953 −10.330 5.941 1.00 33.20 . 1 331 ATOM C CB PRO A 65 . 44.470 −8.339 6.945 1.00 34.59 . 1 332 ATOM C CG PRO A 65 . 44.170 −6.967 7.484 1.00 34.87 . 1 333 ATOM C CD PRO A 65 . 44.959 −6.079 6.556 1.00 34.13 . 1 334 ATOM N N SER A 66 . 46.258 −8.869 4.371 1.00 35.29 . 1 335 ATOM C CA SER A 66 . 46.659 −9.711 3.246 1.00 36.11 . 1 336 ATOM C C SER A 66 . 48.162 −9.930 3.264 1.00 36.21 . 1 337 ATOM O O SER A 66 . 48.640 −11.063 3.157 1.00 36.71 . 1 338 ATOM C CB SER A 66 . 46.260 −9.047 1.923 1.00 36.57 . 1 339 ATOM O OG SER A 66 . 44.897 −8.656 1.953 1.00 37.80 . 1 340 ATOM N N GLU A 67 . 48.902 −8.833 3.391 1.00 36.33 . 1 341 ATOM C CA GLU A 67 . 50.359 −8.882 3.432 1.00 36.56 . 1 342 ATOM C C GLU A 67 . 50.812 −9.789 4.571 1.00 35.85 . 1 343 ATOM O O GLU A 67 . 51.696 −10.613 4.406 1.00 35.54 . 1 344 ATOM C CB GLU A 67 . 50.940 −7.487 3.674 1.00 37.95 . 1 345 ATOM C CG GLU A 67 . 50.510 −6.411 2.701 1.00 39.99 . 1 346 ATOM C CD GLU A 67 . 51.176 −5.079 3.010 1.00 40.83 . 1 347 ATOM O OE1 GLU A 67 . 52.414 −4.991 2.869 1.00 42.18 . 1 348 ATOM O OE2 GLU A 67 . 50.469 −4.124 3.401 1.00 41.64 . 1 349 ATOM N N ILE A 68 . 50.205 −9.602 5.738 1.00 35.60 . 1 350 ATOM C CA ILE A 68 . 50.531 −10.395 6.922 1.00 35.27 . 1 351 ATOM C C ILE A 68 . 50.183 −11.862 6.665 1.00 35.46 . 1 352 ATOM O O ILE A 68 . 50.965 −12.760 6.958 1.00 35.52 . 1 353 ATOM C CB ILE A 68 . 49.749 −9.853 8.154 1.00 34.20 . 1 354 ATOM C CG1 ILE A 68 . 50.106 −8.379 8.370 1.00 34.05 . 1 355 ATOM C CG2 ILE A 68 . 50.108 −10.629 9.411 1.00 34.41 . 1 356 ATOM C CD1 ILE A 68 . 49.171 −7.648 9.317 1.00 34.24 . 1 357 ATOM N N ALA A 69 . 49.009 −12.095 6.094 1.00 36.41 . 1 358 ATOM C CA ALA A 69 . 48.561 −13.451 5.795 1.00 37.59 . 1 359 ATOM C C ALA A 69 . 49.534 −14.197 4.885 1.00 38.36 . 1 360 ATOM O O ALA A 69 . 49.729 −15.406 5.020 1.00 39.01 . 1 361 ATOM C CB ALA A 69 . 47.177 −13.409 5.156 1.00 36.71 . 1 362 ATOM N N SER A 70 . 50.152 −13.474 3.963 1.00 39.84 . 1 363 ATOM C CA SER A 70 . 51.083 −14.092 3.030 1.00 41.47 . 1 364 ATOM C C SER A 70 . 52.405 −14.486 3.676 1.00 42.15 . 1 365 ATOM O O SER A 70 . 53.179 −15.252 3.102 1.00 42.18 . 1 366 ATOM C CB SER A 70 . 51.353 −13.152 1.860 1.00 42.04 . 1 367 ATOM O OG SER A 70 . 51.990 −11.968 2.302 1.00 43.58 . 1 368 ATOM N N LYS A 71 . 52.661 −13.974 4.875 1.00 42.53 . 1 369 ATOM C CA LYS A 71 . 53.903 −14.288 5.560 1.00 43.00 . 1 370 ATOM C C LYS A 71 . 53.777 −15.526 6.425 1.00 43.36 . 1 371 ATOM O O LYS A 71 . 54.773 −16.041 6.916 1.00 43.21 . 1 372 ATOM C CB LYS A 71 . 54.360 −13.095 6.403 1.00 43.07 . 1 373 ATOM C CG LYS A 71 . 54.606 −11.831 5.587 1.00 42.88 . 1 374 ATOM C CD LYS A 71 . 55.657 −12.042 4.502 1.00 43.32 . 1 375 ATOM C CE LYS A 71 . 55.859 −10.766 3.697 1.00 44.19 . 1 376 ATOM N NZ LYS A 71 . 56.737 −10.943 2.504 1.00 44.38 . 1 377 ATOM N N LEU A 72 . 52.551 −16.003 6.609 1.00 44.47 . 1 378 ATOM C CA LEU A 72 . 52.313 −17.205 7.402 1.00 46.18 . 1 379 ATOM C C LEU A 72 . 52.603 −18.420 6.525 1.00 47.85 . 1 380 ATOM O O LEU A 72 . 52.758 −18.284 5.314 1.00 47.28 . 1 381 ATOM C CB LEU A 72 . 50.860 −17.249 7.884 1.00 46.07 . 1 382 ATOM C CG LEU A 72 . 50.430 −16.197 8.909 1.00 46.04 . 1 383 ATOM C CD1 LEU A 72 . 48.947 −16.318 9.176 1.00 46.31 . 1 384 ATOM C CD2 LEU A 72 . 51.221 −16.383 10.196 1.00 46.37 . 1 385 ATOM N N PRO A 73 . 52.686 −19.622 7.125 1.00 49.38 . 1 386 ATOM C CA PRO A 73 . 52.960 −20.843 6.359 1.00 50.97 . 1 387 ATOM C C PRO A 73 . 52.012 −21.004 5.172 1.00 52.47 . 1 388 ATOM O O PRO A 73 . 50.860 −20.574 5.224 1.00 53.04 . 1 389 ATOM C CB PRO A 73 . 52.776 −21.943 7.397 1.00 50.55 . 1 390 ATOM C CG PRO A 73 . 53.266 −21.291 8.638 1.00 50.40 . 1 391 ATOM C CD PRO A 73 . 52.611 −19.923 8.565 1.00 50.03 . 1 392 ATOM N N ALA A 74 . 52.503 −21.624 4.104 1.00 53.94 . 1 393 ATOM C CA ALA A 74 . 51.700 −21.830 2.903 1.00 55.01 . 1 394 ATOM C C ALA A 74 . 50.456 −22.670 3.180 1.00 55.91 . 1 395 ATOM O O ALA A 74 . 49.377 −22.389 2.657 1.00 55.92 . 1 396 ATOM C CB ALA A 74 . 52.545 −22.494 1.828 1.00 55.41 . 1 397 ATOM N N SER A 75 . 50.612 −23.692 4.014 1.00 56.37 . 1 398 ATOM C CA SER A 75 . 49.513 −24.588 4.356 1.00 57.28 . 1 399 ATOM C C SER A 75 . 48.391 −23.940 5.163 1.00 57.65 . 1 400 ATOM O O SER A 75 . 47.308 −24.509 5.290 1.00 57.67 . 1 401 ATOM C CB SER A 75 . 50.051 −25.789 5.134 1.00 57.60 . 1 402 ATOM O OG SER A 75 . 50.632 −25.379 6.360 1.00 58.46 . 1 403 ATOM N N THR A 76 . 48.643 −22.754 5.705 1.00 58.09 . 1 404 ATOM C CA THR A 76 . 47.640 −22.065 6.514 1.00 58.64 . 1 405 ATOM C C THR A 76 . 46.841 −21.057 5.702 1.00 59.24 . 1 406 ATOM O O THR A 76 . 45.852 −20.505 6.184 1.00 59.72 . 1 407 ATOM C CB THR A 76 . 48.297 −21.295 7.680 1.00 58.52 . 1 408 ATOM O OG1 THR A 76 . 49.021 −20.175 7.158 1.00 58.07 . 1 409 ATOM C CG2 THR A 76 . 49.259 −22.191 8.442 1.00 58.06 . 1 410 ATOM N N GLN A 77 . 47.264 −20.828 4.466 1.00 59.68 . 1 411 ATOM C CA GLN A 77 . 46.608 −19.848 3.615 1.00 60.27 . 1 412 ATOM C C GLN A 77 . 45.363 −20.293 2.855 1.00 60.00 . 1 413 ATOM O O GLN A 77 . 45.436 −21.084 1.916 1.00 60.70 . 1 414 ATOM C CB GLN A 77 . 47.630 −19.274 2.632 1.00 60.93 . 1 415 ATOM C CG GLN A 77 . 48.760 −18.517 3.313 1.00 62.02 . 1 416 ATOM C CD GLN A 77 . 49.868 −18.139 2.359 1.00 62.80 . 1 417 ATOM O OE1 GLN A 77 . 49.622 −17.558 1.302 1.00 63.33 . 1 418 ATOM N NE2 GLN A 77 . 51.103 −18.461 2.729 1.00 63.34 . 1 419 ATOM N N HIS A 78 . 44.218 −19.771 3.277 1.00 59.37 . 1 420 ATOM C CA HIS A 78 . 42.950 −20.053 2.624 1.00 58.43 . 1 421 ATOM C C HIS A 78 . 42.316 −18.709 2.274 1.00 57.63 . 1 422 ATOM O O HIS A 78 . 42.728 −17.668 2.780 1.00 57.59 . 1 423 ATOM C CB HIS A 78 . 42.022 −20.862 3.534 1.00 58.77 . 1 424 ATOM C CG HIS A 78 . 41.944 −20.346 4.936 1.00 59.28 . 1 425 ATOM N ND1 HIS A 78 . 42.923 −20.592 5.874 1.00 59.40 . 1 426 ATOM C CD2 HIS A 78 . 41.001 −19.600 5.560 1.00 59.24 . 1 427 ATOM C CE1 HIS A 78 . 42.586 −20.023 7.018 1.00 59.38 . 1 428 ATOM N NE2 HIS A 78 . 41.424 −19.414 6.855 1.00 59.50 . 1 429 ATOM N N SER A 79 . 41.318 −18.738 1.403 1.00 56.50 . 1 430 ATOM C CA SER A 79 . 40.642 −17.528 0.953 1.00 55.28 . 1 431 ATOM C C SER A 79 . 40.265 −16.530 2.044 1.00 54.23 . 1 432 ATOM O O SER A 79 . 40.449 −15.326 1.877 1.00 53.85 . 1 433 ATOM C CB SER A 79 . 39.381 −17.905 0.172 1.00 55.21 . 1 434 ATOM O OG SER A 79 . 38.498 −18.662 0.979 1.00 55.91 . 1 435 ATOM N N ASP A 80 . 39.743 −17.035 3.157 1.00 53.30 . 1 436 ATOM C CA ASP A 80 . 39.291 −16.183 4.254 1.00 52.43 . 1 437 ATOM C C ASP A 80 . 40.319 −15.886 5.352 1.00 50.80 . 1 438 ATOM O O ASP A 80 . 39.956 −15.386 6.415 1.00 50.75 . 1 439 ATOM C CB ASP A 80 . 38.033 −16.801 4.876 1.00 53.15 . 1 440 ATOM C CG ASP A 80 . 37.317 −15.856 5.826 1.00 54.49 . 1 441 ATOM O OD1 ASP A 80 . 36.929 −14.747 5.391 1.00 55.52 . 1 442 ATOM O OD2 ASP A 80 . 37.135 −16.225 7.009 1.00 54.80 . 1 443 ATOM N N LEU A 81 . 41.592 −16.174 5.103 1.00 49.31 . 1 444 ATOM C CA LEU A 81 . 42.627 −15.917 6.105 1.00 47.62 . 1 445 ATOM C C LEU A 81 . 42.789 −14.420 6.411 1.00 46.47 . 1 446 ATOM O O LEU A 81 . 42.795 −14.014 7.572 1.00 45.97 . 1 447 ATOM C CB LEU A 81 . 43.971 −16.502 5.658 1.00 47.55 . 1 448 ATOM C CG LEU A 81 . 45.117 −16.424 6.677 1.00 47.63 . 1 449 ATOM C CD1 LEU A 81 . 44.805 −17.315 7.877 1.00 47.60 . 1 450 ATOM C CD2 LEU A 81 . 46.419 −16.862 6.032 1.00 47.56 . 1 451 ATOM N N PRO A 82 . 42.920 −13.578 5.373 1.00 45.34 . 1 452 ATOM C CA PRO A 82 . 43.079 −12.141 5.620 1.00 44.15 . 1 453 ATOM C C PRO A 82 . 41.967 −11.550 6.486 1.00 43.66 . 1 454 ATOM O O PRO A 82 . 42.225 −10.719 7.361 1.00 43.39 . 1 455 ATOM C CB PRO A 82 . 43.086 −11.547 4.212 1.00 44.23 . 1 456 ATOM C CG PRO A 82 . 43.708 −12.645 3.395 1.00 44.50 . 1 457 ATOM C CD PRO A 82 . 42.998 −13.871 3.931 1.00 44.99 . 1 458 ATOM N N ASN A 83 . 40.733 −11.980 6.248 1.00 42.54 . 1 459 ATOM C CA ASN A 83 . 39.606 −11.455 7.008 1.00 42.16 . 1 460 ATOM C C ASN A 83 . 39.655 −11.882 8.468 1.00 40.56 . 1 461 ATOM O O ASN A 83 . 39.321 −11.104 9.357 1.00 39.67 . 1 462 ATOM C CB ASN A 83 . 38.278 −11.902 6.397 1.00 44.56 . 1 463 ATOM C CG ASN A 83 . 37.114 −11.055 6.873 1.00 46.49 . 1 464 ATOM O OD1 ASN A 83 . 37.131 −9.835 6.724 1.00 48.47 . 1 465 ATOM N ND2 ASN A 83 . 36.100 −11.690 7.444 1.00 48.59 . 1 466 ATOM N N ARG A 84 . 40.079 −13.117 8.704 1.00 39.08 . 1 467 ATOM C CA ARG A 84 . 40.167 −13.646 10.056 1.00 38.51 . 1 468 ATOM C C ARG A 84 . 41.247 −12.930 10.850 1.00 37.18 . 1 469 ATOM O O ARG A 84 . 41.063 −12.639 12.030 1.00 37.07 . 1 470 ATOM C CB ARG A 84 . 40.457 −15.140 10.012 1.00 38.96 . 1 471 ATOM C CG ARG A 84 . 39.344 −15.921 9.359 1.00 40.33 . 1 472 ATOM C CD ARG A 84 . 39.610 −17.411 9.332 1.00 41.15 . 1 473 ATOM N NE ARG A 84 . 38.430 −18.101 8.822 1.00 42.31 . 1 474 ATOM C CZ ARG A 84 . 38.289 −19.419 8.772 1.00 42.41 . 1 475 ATOM N NH1 ARG A 84 . 39.263 −20.212 9.198 1.00 42.22 . 1 476 ATOM N NH2 ARG A 84 . 37.158 −19.938 8.313 1.00 43.09 . 1 477 ATOM N N LEU A 85 . 42.370 −12.649 10.195 1.00 35.82 . 1 478 ATOM C CA LEU A 85 . 43.466 −11.952 10.843 1.00 35.13 . 1 479 ATOM C C LEU A 85 . 43.026 −10.542 11.193 1.00 34.75 . 1 480 ATOM O O LEU A 85 . 43.299 −10.047 12.291 1.00 34.50 . 1 481 ATOM C CB LEU A 85 . 44.686 −11.900 9.922 1.00 34.45 . 1 482 ATOM C CG LEU A 85 . 45.379 −13.237 9.643 1.00 34.19 . 1 483 ATOM C CD1 LEU A 85 . 46.540 −13.026 8.694 1.00 33.94 . 1 484 ATOM C CD2 LEU A 85 . 45.871 −13.842 10.945 1.00 34.42 . 1 485 ATOM N N ASP A 86 . 42.322 −9.907 10.261 1.00 34.13 . 1 486 ATOM C CA ASP A 86 . 41.851 −8.549 10.470 1.00 34.62 . 1 487 ATOM C C ASP A 86 . 40.941 −8.429 11.682 1.00 33.71 . 1 488 ATOM O O ASP A 86 . 40.941 −7.407 12.363 1.00 32.73 . 1 489 ATOM C CB ASP A 86 . 41.113 −8.037 9.234 1.00 36.00 . 1 490 ATOM C CG ASP A 86 . 40.735 −6.576 9.358 1.00 37.11 . 1 491 ATOM O OD1 ASP A 86 . 41.638 −5.744 9.598 1.00 38.57 . 1 492 ATOM O OD2 ASP A 86 . 39.539 −6.258 9.227 1.00 40.00 . 1 493 ATOM N N ARG A 87 . 40.158 −9.469 11.938 1.00 33.06 . 1 494 ATOM C CA ARG A 87 . 39.249 −9.464 13.073 1.00 33.11 . 1 495 ATOM C C ARG A 87 . 40.048 −9.477 14.380 1.00 32.10 . 1 496 ATOM O O ARG A 87 . 39.646 −8.855 15.359 1.00 32.10 . 1 497 ATOM C CB ARG A 87 . 38.315 −10.673 12.984 1.00 34.25 . 1 498 ATOM C CG ARG A 87 . 37.575 −10.712 11.659 1.00 36.54 . 1 499 ATOM C CD ARG A 87 . 36.767 −11.979 11.481 1.00 38.37 . 1 500 ATOM N NE ARG A 87 . 35.646 −12.075 12.411 1.00 39.29 . 1 501 ATOM C CZ ARG A 87 . 34.778 −13.079 12.401 1.00 39.60 . 1 502 ATOM N NH1 ARG A 87 . 34.916 −14.052 11.510 1.00 39.92 . 1 503 ATOM N NH2 ARG A 87 . 33.782 −13.117 13.276 1.00 39.72 . 1 504 HETA N N MSE A 88 . 41.181 −10.178 14.372 1.00 31.10 . 1 505 HETA C CA MSE A 88 . 42.066 −10.265 15.532 1.00 30.33 . 1 506 HETA C C MSE A 88 . 42.830 −8.942 15.673 1.00 29.91 . 1 507 HETA O O MSE A 88 . 42.942 −8.378 16.755 1.00 28.30 . 1 508 HETA C CB MSE A 88 . 43.101 −11.388 15.354 1.00 29.82 . 1 509 HETA C CG MSE A 88 . 42.560 −12.806 15.276 1.00 31.12 . 1 510 HETA SE SE MSE A 88 . 43.925 −14.029 15.142 1.00 32.49 . 1 511 HETA C CE MSE A 88 . 44.618 −13.518 13.720 1.00 32.35 . 1 512 ATOM N N LEU A 89 . 43.357 −8.467 14.556 1.00 29.18 . 1 513 ATOM C CA LEU A 89 . 44.126 −7.236 14.540 1.00 29.74 . 1 514 ATOM C C LEU A 89 . 43.302 −6.062 15.053 1.00 29.69 . 1 515 ATOM O O LEU A 89 . 43.833 −5.186 15.744 1.00 30.41 . 1 516 ATOM C CB LEU A 89 . 44.647 −6.978 13.119 1.00 29.70 . 1 517 ATOM C CG LEU A 89 . 45.544 −8.090 12.558 1.00 29.40 . 1 518 ATOM C CD1 LEU A 89 . 45.900 −7.790 11.108 1.00 28.22 . 1 519 ATOM C CD2 LEU A 89 . 46.808 −8.231 13.400 1.00 28.98 . 1 520 ATOM N N ARG A 90 . 42.007 −6.054 14.735 1.00 28.98 . 1 521 ATOM C CA ARG A 90 . 41.106 −4.994 15.194 1.00 29.57 . 1 522 ATOM C C ARG A 90 . 41.100 −4.935 16.726 1.00 29.31 . 1 523 ATOM O O ARG A 90 . 41.156 −3.861 17.311 1.00 29.14 . 1 524 ATOM C CB ARG A 90 . 39.674 −5.261 14.727 1.00 30.47 . 1 525 ATOM C CG ARG A 90 . 39.110 −4.269 13.725 1.00 32.26 . 1 526 ATOM C CD ARG A 90 . 37.675 −4.655 13.401 1.00 33.34 . 1 527 ATOM N NE ARG A 90 . 37.100 −3.861 12.321 1.00 34.06 . 1 528 ATOM C CZ ARG A 90 . 36.548 −2.662 12.465 1.00 33.70 . 1 529 ATOM N NH1 ARG A 90 . 36.482 −2.083 13.658 1.00 33.57 . 1 530 ATOM N NH2 ARG A 90 . 36.054 −2.043 11.397 1.00 34.54 . 1 531 ATOM N N LEU A 91 . 40.997 −6.100 17.360 1.00 28.84 . 1 532 ATOM C CA LEU A 91 . 40.981 −6.188 18.821 1.00 28.69 . 1 533 ATOM C C LEU A 91 . 42.302 −5.675 19.359 1.00 28.31 . 1 534 ATOM O O LEU A 91 . 42.336 −4.862 20.275 1.00 27.91 . 1 535 ATOM C CB LEU A 91 . 40.798 −7.640 19.277 1.00 29.39 . 1 536 ATOM C CG LEU A 91 . 39.846 −7.918 20.442 1.00 30.65 . 1 537 ATOM C CD1 LEU A 91 . 40.239 −9.230 21.095 1.00 30.67 . 1 538 ATOM C CD2 LEU A 91 . 39.884 −6.783 21.455 1.00 31.42 . 1 539 ATOM N N LEU A 92 . 43.392 −6.158 18.778 1.00 28.54 . 1 540 ATOM C CA LEU A 92 . 44.720 −5.748 19.207 1.00 29.26 . 1 541 ATOM C C LEU A 92 . 44.949 −4.244 19.077 1.00 29.64 . 1 542 ATOM O O LEU A 92 . 45.629 −3.644 19.909 1.00 29.13 . 1 543 ATOM C CB LEU A 92 . 45.773 −6.538 18.435 1.00 29.24 . 1 544 ATOM C CG LEU A 92 . 45.788 −8.015 18.858 1.00 29.78 . 1 545 ATOM C CD1 LEU A 92 . 46.683 −8.807 17.934 1.00 29.13 . 1 546 ATOM C CD2 LEU A 92 . 46.265 −8.139 20.310 1.00 29.94 . 1 547 ATOM N N ALA A 93 . 44.378 −3.633 18.042 1.00 29.90 . 1 548 ATOM C CA ALA A 93 . 44.514 −2.194 17.860 1.00 29.73 . 1 549 ATOM C C ALA A 93 . 43.633 −1.477 18.879 1.00 29.56 . 1 550 ATOM O O ALA A 93 . 43.980 −0.401 19.361 1.00 29.33 . 1 551 ATOM C CB ALA A 93 . 44.110 −1.784 16.430 1.00 29.38 . 1 552 ATOM N N SER A 94 . 42.487 −2.070 19.203 1.00 29.59 . 1 553 ATOM C CA SER A 94 . 41.575 −1.465 20.168 1.00 29.85 . 1 554 ATOM C C SER A 94 . 42.212 −1.438 21.562 1.00 30.57 . 1 555 ATOM O O SER A 94 . 41.818 −0.651 22.422 1.00 29.17 . 1 556 ATOM C CB SER A 94 . 40.253 −2.237 20.210 1.00 30.54 . 1 557 ATOM O OG SER A 94 . 39.599 −2.191 18.948 1.00 32.32 . 1 558 ATOM N N TYR A 95 . 43.202 −2.300 21.772 1.00 30.82 . 1 559 ATOM C CA TYR A 95 . 43.898 −2.348 23.051 1.00 32.09 . 1 560 ATOM C C TYR A 95 . 45.227 −1.615 23.038 1.00 32.65 . 1 561 ATOM O O TYR A 95 . 46.005 −1.735 23.969 1.00 33.87 . 1 562 ATOM C CB TYR A 95 . 44.098 −3.799 23.498 1.00 32.37 . 1 563 ATOM C CG TYR A 95 . 42.913 −4.295 24.283 1.00 33.05 . 1 564 ATOM C CD1 TYR A 95 . 41.890 −5.013 23.670 1.00 33.31 . 1 565 ATOM C CD2 TYR A 95 . 42.765 −3.953 25.628 1.00 34.03 . 1 566 ATOM C CE1 TYR A 95 . 40.747 −5.366 24.369 1.00 33.62 . 1 567 ATOM C CE2 TYR A 95 . 41.624 −4.304 26.338 1.00 34.44 . 1 568 ATOM C CZ TYR A 95 . 40.620 −5.005 25.703 1.00 35.12 . 1 569 ATOM O OH TYR A 95 . 39.475 −5.313 26.401 1.00 36.90 . 1 570 ATOM N N SER A 96 . 45.476 −0.847 21.981 1.00 33.24 . 1 571 ATOM C CA SER A 96 . 46.701 −0.069 21.844 1.00 33.41 . 1 572 ATOM C C SER A 96 . 47.985 −0.872 21.666 1.00 32.81 . 1 573 ATOM O O SER A 96 . 49.077 −0.369 21.919 1.00 32.81 . 1 574 ATOM C CB SER A 96 . 46.854 0.884 23.030 1.00 34.39 . 1 575 ATOM O OG SER A 96 . 45.940 1.965 22.924 1.00 36.87 . 1 576 ATOM N N VAL A 97 . 47.860 −2.117 21.230 1.00 31.53 . 1 577 ATOM C CA VAL A 97 . 49.031 −2.948 20.997 1.00 31.04 . 1 578 ATOM C C VAL A 97 . 49.528 −2.670 19.575 1.00 31.18 . 1 579 ATOM O O VAL A 97 . 50.720 −2.733 19.274 1.00 30.49 . 1 580 ATOM C CB VAL A 97 . 48.676 −4.438 21.123 1.00 30.47 . 1 581 ATOM C CG1 VAL A 97 . 49.905 −5.284 20.872 1.00 30.79 . 1 582 ATOM C CG2 VAL A 97 . 48.101 −4.713 22.495 1.00 30.32 . 1 583 ATOM N N LEU A 98 . 48.588 −2.350 18.702 1.00 31.36 . 1 584 ATOM C CA LEU A 98 . 48.910 −2.059 17.318 1.00 31.88 . 1 585 ATOM C C LEU A 98 . 48.377 −0.697 16.954 1.00 32.03 . 1 586 ATOM O O LEU A 98 . 47.402 −0.235 17.540 1.00 32.29 . 1 587 ATOM C CB LEU A 98 . 48.256 −3.090 16.391 1.00 30.39 . 1 588 ATOM C CG LEU A 98 . 48.660 −4.548 16.588 1.00 29.46 . 1 589 ATOM C CD1 LEU A 98 . 47.876 −5.430 15.604 1.00 29.47 . 1 590 ATOM C CD2 LEU A 98 . 50.144 −4.691 16.379 1.00 27.63 . 1 591 ATOM N N THR A 99 . 49.033 −0.051 16.001 1.00 32.61 . 1 592 ATOM C CA THR A 99 . 48.569 1.239 15.520 1.00 34.13 . 1 593 ATOM C C THR A 99 . 47.771 0.859 14.270 1.00 34.71 . 1 594 ATOM O O THR A 99 . 48.023 −0.183 13.661 1.00 33.87 . 1 595 ATOM C CB THR A 99 . 49.744 2.177 15.124 1.00 34.07 . 1 596 ATOM O OG1 THR A 99 . 50.525 1.564 14.096 1.00 34.67 . 1 597 ATOM C CG2 THR A 99 . 50.636 2.457 16.327 1.00 34.55 . 1 598 ATOM N N SER A 100 . 46.807 1.688 13.894 1.00 35.75 . 1 599 ATOM C CA SER A 100 . 45.996 1.388 12.727 1.00 37.35 . 1 600 ATOM C C SER A 100 . 45.647 2.631 11.917 1.00 37.64 . 1 601 ATOM O O SER A 100 . 45.475 3.716 12.464 1.00 36.82 . 1 602 ATOM C CB SER A 100 . 44.705 0.695 13.174 1.00 38.03 . 1 603 ATOM O OG SER A 100 . 43.928 0.287 12.067 1.00 39.59 . 1 604 ATOM N N THR A 101 . 45.552 2.461 10.603 1.00 38.90 . 1 605 ATOM C CA THR A 101 . 45.177 3.549 9.706 1.00 39.91 . 1 606 ATOM C C THR A 101 . 44.727 2.950 8.375 1.00 40.69 . 1 607 ATOM O O THR A 101 . 44.663 1.725 8.229 1.00 40.04 . 1 608 ATOM C CB THR A 101 . 46.350 4.547 9.473 1.00 40.35 . 1 609 ATOM O OG1 THR A 101 . 45.887 5.646 8.674 1.00 40.87 . 1 610 ATOM C CG2 THR A 101 . 47.515 3.875 8.776 1.00 39.50 . 1 611 ATOM N N THR A 102 . 44.388 3.803 7.415 1.00 41.57 . 1 612 ATOM C CA THR A 102 . 43.952 3.310 6.113 1.00 43.12 . 1 613 ATOM C C THR A 102 . 44.934 3.724 5.038 1.00 43.60 . 1 614 ATOM O O THR A 102 . 45.574 4.775 5.134 1.00 43.91 . 1 615 ATOM C CB THR A 102 . 42.540 3.822 5.741 1.00 43.62 . 1 616 ATOM O OG1 THR A 102 . 42.510 5.254 5.790 1.00 44.91 . 1 617 ATOM C CG2 THR A 102 . 41.507 3.258 6.704 1.00 44.16 . 1 618 ATOM N N ARG A 103 . 45.062 2.876 4.026 1.00 43.78 . 1 619 ATOM C CA ARG A 103 . 45.970 3.116 2.917 1.00 44.23 . 1 620 ATOM C C ARG A 103 . 45.183 3.059 1.610 1.00 44.37 . 1 621 ATOM O O ARG A 103 . 44.333 2.187 1.426 1.00 44.18 . 1 622 ATOM C CB ARG A 103 . 47.069 2.053 2.923 1.00 44.54 . 1 623 ATOM C CG ARG A 103 . 48.082 2.181 1.804 1.00 45.06 . 1 624 ATOM C CD ARG A 103 . 49.215 1.187 1.986 1.00 45.30 . 1 625 ATOM N NE ARG A 103 . 48.754 −0.195 1.907 1.00 45.35 . 1 626 ATOM C CZ ARG A 103 . 49.537 −1.255 2.093 1.00 46.09 . 1 627 ATOM N NH1 ARG A 103 . 50.821 −1.095 2.378 1.00 46.01 . 1 628 ATOM N NH2 ARG A 103 . 49.040 −2.481 1.981 1.00 45.76 . 1 629 ATOM N N THR A 104 . 45.460 4.000 0.713 1.00 44.48 . 1 630 ATOM C CA THR A 104 . 44.776 4.063 −0.572 1.00 44.45 . 1 631 ATOM C C THR A 104 . 45.559 3.275 −1.602 1.00 44.51 . 1 632 ATOM O O THR A 104 . 46.768 3.458 −1.747 1.00 44.79 . 1 633 ATOM C CB THR A 104 . 44.642 5.515 −1.061 1.00 44.80 . 1 634 ATOM O OG1 THR A 104 . 43.851 6.257 −0.125 1.00 45.08 . 1 635 ATOM C CG2 THR A 104 . 43.972 5.562 −2.428 1.00 44.56 . 1 636 ATOM N N ILE A 105 . 44.878 2.393 −2.319 1.00 44.80 . 1 637 ATOM C CA ILE A 105 . 45.566 1.596 −3.324 1.00 45.51 . 1 638 ATOM C C ILE A 105 . 45.484 2.234 −4.713 1.00 45.70 . 1 639 ATOM O O ILE A 105 . 44.790 3.230 −4.914 1.00 45.46 . 1 640 ATOM C CB ILE A 105 . 45.015 0.147 −3.373 1.00 45.71 . 1 641 ATOM C CG1 ILE A 105 . 43.633 0.118 −4.014 1.00 46.46 . 1 642 ATOM C CG2 ILE A 105 . 44.911 −0.415 −1.952 1.00 46.02 . 1 643 ATOM C CD1 ILE A 105 . 43.137 −1.282 −4.284 1.00 47.06 . 1 644 ATOM N N GLU A 106 . 46.211 1.644 −5.654 1.00 45.94 . 1 645 ATOM C CA GLU A 106 . 46.300 2.098 −7.038 1.00 46.51 . 1 646 ATOM C C GLU A 106 . 45.004 2.573 −7.708 1.00 46.11 . 1 647 ATOM O O GLU A 106 . 44.990 3.600 −8.385 1.00 45.81 . 1 648 ATOM C CB GLU A 106 . 46.918 0.978 −7.879 1.00 47.60 . 1 649 ATOM C CG GLU A 106 . 47.493 1.438 −9.193 1.00 49.86 . 1 650 ATOM C CD GLU A 106 . 48.029 0.293 −10.026 1.00 50.72 . 1 651 ATOM O OE1 GLU A 106 . 47.212 −0.485 −10.564 1.00 51.89 . 1 652 ATOM O OE2 GLU A 106 . 49.269 0.171 −10.141 1.00 51.69 . 1 653 ATOM N N ASP A 107 . 43.920 1.827 −7.532 1.00 45.99 . 1 654 ATOM C CA ASP A 107 . 42.651 2.187 −8.157 1.00 45.64 . 1 655 ATOM C C ASP A 107 . 41.827 3.135 −7.300 1.00 45.08 . 1 656 ATOM O O ASP A 107 . 40.641 3.349 −7.553 1.00 45.01 . 1 657 ATOM C CB ASP A 107 . 41.838 0.925 −8.463 1.00 46.14 . 1 658 ATOM C CG ASP A 107 . 41.391 0.203 −7.208 1.00 47.14 . 1 659 ATOM O OD1 ASP A 107 . 40.724 −0.847 −7.328 1.00 47.80 . 1 660 ATOM O OD2 ASP A 107 . 41.702 0.687 −6.101 1.00 47.32 . 1 661 ATOM N N GLY A 108 . 42.462 3.707 −6.285 1.00 44.33 . 1 662 ATOM C CA GLY A 108 . 41.764 4.629 −5.411 1.00 44.17 . 1 663 ATOM C C GLY A 108 . 41.141 3.945 −4.208 1.00 44.35 . 1 664 ATOM O O GLY A 108 . 40.788 4.604 −3.235 1.00 44.88 . 1 665 ATOM N N GLY A 109 . 40.995 2.627 −4.270 1.00 43.90 . 1 666 ATOM C CA GLY A 109 . 40.407 1.908 −3.155 1.00 43.43 . 1 667 ATOM C C GLY A 109 . 41.209 2.096 −1.880 1.00 42.77 . 1 668 ATOM O O GLY A 109 . 42.373 2.501 −1.919 1.00 42.75 . 1 669 ATOM N N ALA A 110 . 40.592 1.802 −0.742 1.00 42.46 . 1 670 ATOM C CA ALA A 110 . 41.273 1.951 0.541 1.00 42.12 . 1 671 ATOM C C ALA A 110 . 41.303 0.629 1.296 1.00 41.59 . 1 672 ATOM O O ALA A 110 . 40.371 −0.165 1.208 1.00 41.86 . 1 673 ATOM C CB ALA A 110 . 40.576 3.020 1.388 1.00 41.46 . 1 674 ATOM N N GLU A 111 . 42.386 0.396 2.030 1.00 41.07 . 1 675 ATOM C CA GLU A 111 . 42.515 −0.823 2.816 1.00 40.08 . 1 676 ATOM C C GLU A 111 . 43.140 −0.494 4.163 1.00 38.81 . 1 677 ATOM O O GLU A 111 . 44.042 0.337 4.255 1.00 38.27 . 1 678 ATOM C CB GLU A 111 . 43.376 −1.852 2.080 1.00 40.61 . 1 679 ATOM C CG GLU A 111 . 44.852 −1.513 2.008 1.00 41.84 . 1 680 ATOM C CD GLU A 111 . 45.638 −2.539 1.216 1.00 42.81 . 1 681 ATOM O OE1 GLU A 111 . 45.180 −3.699 1.128 1.00 43.66 . 1 682 ATOM O OE2 GLU A 111 . 46.718 −2.193 0.691 1.00 43.26 . 1 683 ATOM N N ARG A 112 . 42.652 −1.149 5.206 1.00 37.76 . 1 684 ATOM C CA ARG A 112 . 43.167 −0.939 6.555 1.00 36.73 . 1 685 ATOM C C ARG A 112 . 44.537 −1.605 6.728 1.00 35.62 . 1 686 ATOM O O ARG A 112 . 44.745 −2.736 6.300 1.00 35.06 . 1 687 ATOM C CB ARG A 112 . 42.162 −1.487 7.576 1.00 37.29 . 1 688 ATOM C CG ARG A 112 . 42.619 −1.416 9.025 1.00 38.35 . 1 689 ATOM C CD ARG A 112 . 41.436 −1.532 9.987 1.00 38.60 . 1 690 ATOM N NE ARG A 112 . 40.628 −2.727 9.752 1.00 39.12 . 1 691 ATOM C CZ ARG A 112 . 39.382 −2.708 9.282 1.00 39.14 . 1 692 ATOM N NH1 ARG A 112 . 38.793 −1.554 8.993 1.00 37.77 . 1 693 ATOM N NH2 ARG A 112 . 38.724 −3.845 9.104 1.00 39.25 . 1 694 ATOM N N VAL A 113 . 45.473 −0.886 7.342 1.00 34.75 . 1 695 ATOM C CA VAL A 113 . 46.822 −1.403 7.578 1.00 34.06 . 1 696 ATOM C C VAL A 113 . 47.169 −1.278 9.057 1.00 33.18 . 1 697 ATOM O O VAL A 113 . 46.580 −0.466 9.765 1.00 33.25 . 1 698 ATOM C CB VAL A 113 . 47.888 −0.645 6.754 1.00 34.34 . 1 699 ATOM C CG1 VAL A 113 . 47.735 −0.983 5.276 1.00 34.78 . 1 700 ATOM C CG2 VAL A 113 . 47.753 0.864 6.987 1.00 34.20 . 1 701 ATOM N N TYR A 114 . 48.127 −2.082 9.510 1.00 32.74 . 1 702 ATOM C CA TYR A 114 . 48.525 −2.089 10.915 1.00 32.27 . 1 703 ATOM C C TYR A 114 . 50.015 −1.962 11.171 1.00 31.81 . 1 704 ATOM O O TYR A 114 . 50.845 −2.414 10.374 1.00 32.23 . 1 705 ATOM C CB TYR A 114 . 48.063 −3.381 11.592 1.00 31.26 . 1 706 ATOM C CG TYR A 114 . 46.576 −3.584 11.622 1.00 30.89 . 1 707 ATOM C CD1 TYR A 114 . 45.917 −4.222 10.572 1.00 30.72 . 1 708 ATOM C CD2 TYR A 114 . 45.823 −3.146 12.709 1.00 30.68 . 1 709 ATOM C CE1 TYR A 114 . 44.545 −4.425 10.607 1.00 30.68 . 1 710 ATOM C CE2 TYR A 114 . 44.452 −3.341 12.757 1.00 30.67 . 1 711 ATOM C CZ TYR A 114 . 43.817 −3.984 11.705 1.00 30.42 . 1 712 ATOM O OH TYR A 114 . 42.465 −4.214 11.777 1.00 29.51 . 1 713 ATOM N N GLY A 115 . 50.334 −1.375 12.320 1.00 31.10 . 1 714 ATOM C CA GLY A 115 . 51.716 −1.217 12.731 1.00 30.16 . 1 715 ATOM C C GLY A 115 . 51.809 −1.531 14.217 1.00 29.44 . 1 716 ATOM O O GLY A 115 . 50.799 −1.797 14.862 1.00 28.88 . 1 717 ATOM N N LEU A 116 . 53.021 −1.514 14.758 1.00 29.71 . 1 718 ATOM C CA LEU A 116 . 53.229 −1.780 16.175 1.00 29.40 . 1 719 ATOM C C LEU A 116 . 53.287 −0.445 16.907 1.00 29.23 . 1 720 ATOM O O LEU A 116 . 53.860 0.513 16.396 1.00 28.74 . 1 721 ATOM C CB LEU A 116 . 54.545 −2.531 16.385 1.00 29.01 . 1 722 ATOM C CG LEU A 116 . 54.664 −3.931 15.774 1.00 30.35 . 1 723 ATOM C CD1 LEU A 116 . 56.042 −4.502 16.073 1.00 29.82 . 1 724 ATOM C CD2 LEU A 116 . 53.581 −4.842 16.341 1.00 29.21 . 1 725 ATOM N N SER A 117 . 52.683 −0.378 18.088 1.00 29.38 . 1 726 ATOM C CA SER A 117 . 52.718 0.847 18.879 1.00 28.88 . 1 727 ATOM C C SER A 117 . 53.933 0.751 19.803 1.00 28.80 . 1 728 ATOM O O SER A 117 . 54.725 −0.185 19.692 1.00 28.91 . 1 729 ATOM C CB SER A 117 . 51.433 1.000 19.709 1.00 29.19 . 1 730 ATOM O OG SER A 117 . 51.321 0.002 20.724 1.00 29.75 . 1 731 HETA N N MSE A 118 . 54.095 1.716 20.702 1.00 28.62 . 1 732 HETA C CA MSE A 118 . 55.222 1.675 21.634 1.00 28.98 . 1 733 HETA C C MSE A 118 . 55.060 0.468 22.550 1.00 28.21 . 1 734 HETA O O MSE A 118 . 56.039 −0.078 23.055 1.00 29.05 . 1 735 HETA C CB MSE A 118 . 55.268 2.935 22.499 1.00 28.82 . 1 736 HETA C CG MSE A 118 . 55.869 4.166 21.837 1.00 30.83 . 1 737 HETA SE SE MSE A 118 . 56.073 5.476 23.098 1.00 29.82 . 1 738 HETA C CE MSE A 118 . 57.544 4.927 23.873 1.00 29.96 . 1 739 ATOM N N VAL A 119 . 53.815 0.066 22.767 1.00 27.22 . 1 740 ATOM C CA VAL A 119 . 53.509 −1.077 23.620 1.00 27.41 . 1 741 ATOM C C VAL A 119 . 53.757 −2.358 22.835 1.00 27.41 . 1 742 ATOM O O VAL A 119 . 54.427 −3.281 23.313 1.00 26.28 . 1 743 ATOM C CB VAL A 119 . 52.036 −1.039 24.072 1.00 27.33 . 1 744 ATOM C CG1 VAL A 119 . 51.722 −2.215 24.986 1.00 28.15 . 1 745 ATOM C CG2 VAL A 119 . 51.751 0.288 24.783 1.00 28.06 . 1 746 ATOM N N GLY A 120 . 53.225 −2.397 21.614 1.00 26.36 . 1 747 ATOM C CA GLY A 120 . 53.380 −3.576 20.778 1.00 25.71 . 1 748 ATOM C C GLY A 120 . 54.792 −4.044 20.490 1.00 25.84 . 1 749 ATOM O O GLY A 120 . 55.011 −5.246 20.306 1.00 25.44 . 1 750 ATOM N N LYS A 121 . 55.757 −3.127 20.446 1.00 25.28 . 1 751 ATOM C CA LYS A 121 . 57.127 −3.514 20.143 1.00 26.01 . 1 752 ATOM C C LYS A 121 . 57.718 −4.502 21.147 1.00 26.47 . 1 753 ATOM O O LYS A 121 . 58.650 −5.240 20.817 1.00 26.29 . 1 754 ATOM C CB LYS A 121 . 58.044 −2.283 20.030 1.00 26.55 . 1 755 ATOM C CG LYS A 121 . 58.404 −1.590 21.338 1.00 26.93 . 1 756 ATOM C CD LYS A 121 . 59.412 −0.455 21.080 1.00 26.84 . 1 757 ATOM C CE LYS A 121 . 59.840 0.269 22.351 1.00 25.39 . 1 758 ATOM N NZ LYS A 121 . 58.701 0.975 22.993 1.00 25.21 . 1 759 ATOM N N TYR A 122 . 57.185 −4.513 22.365 1.00 26.36 . 1 760 ATOM C CA TYR A 122 . 57.679 −5.432 23.387 1.00 27.38 . 1 761 ATOM C C TYR A 122 . 57.246 −6.888 23.120 1.00 28.53 . 1 762 ATOM O O TYR A 122 . 57.612 −7.804 23.863 1.00 27.54 . 1 763 ATOM C CB TYR A 122 . 57.209 −4.984 24.768 1.00 26.69 . 1 764 ATOM C CG TYR A 122 . 57.928 −3.743 25.281 1.00 26.89 . 1 765 ATOM C CD1 TYR A 122 . 57.351 −2.477 25.173 1.00 26.70 . 1 766 ATOM C CD2 TYR A 122 . 59.192 −3.844 25.861 1.00 28.39 . 1 767 ATOM C CE1 TYR A 122 . 58.018 −1.335 25.637 1.00 27.65 . 1 768 ATOM C CE2 TYR A 122 . 59.868 −2.707 26.326 1.00 28.55 . 1 769 ATOM C CZ TYR A 122 . 59.275 −1.468 26.212 1.00 27.75 . 1 770 ATOM O OH TYR A 122 . 59.941 −0.369 26.690 1.00 29.06 . 1 771 ATOM N N LEU A 123 . 56.474 −7.091 22.057 1.00 28.85 . 1 772 ATOM C CA LEU A 123 . 56.017 −8.430 21.698 1.00 29.85 . 1 773 ATOM C C LEU A 123 . 56.854 −9.013 20.566 1.00 30.21 . 1 774 ATOM O O LEU A 123 . 56.523 −10.063 20.010 1.00 31.22 . 1 775 ATOM C CB LEU A 123 . 54.542 −8.395 21.295 1.00 29.51 . 1 776 ATOM C CG LEU A 123 . 53.605 −7.868 22.375 1.00 29.58 . 1 777 ATOM C CD1 LEU A 123 . 52.209 −7.751 21.825 1.00 30.25 . 1 778 ATOM C CD2 LEU A 123 . 53.633 −8.800 23.584 1.00 30.71 . 1 779 ATOM N N VAL A 124 . 57.938 −8.320 20.231 1.00 30.71 . 1 780 ATOM C CA VAL A 124 . 58.848 −8.744 19.176 1.00 31.37 . 1 781 ATOM C C VAL A 124 . 60.130 −9.287 19.810 1.00 32.65 . 1 782 ATOM O O VAL A 124 . 60.823 −8.579 20.547 1.00 31.12 . 1 783 ATOM C CB VAL A 124 . 59.209 −7.569 18.246 1.00 31.01 . 1 784 ATOM C CG1 VAL A 124 . 60.098 −8.057 17.109 1.00 31.04 . 1 785 ATOM C CG2 VAL A 124 . 57.944 −6.931 17.706 1.00 30.83 . 1 786 ATOM N N PRO A 125 . 60.462 −10.555 19.527 1.00 33.85 . 1 787 ATOM C CA PRO A 125 . 61.657 −11.209 20.069 1.00 35.56 . 1 788 ATOM C C PRO A 125 . 62.945 −10.391 20.006 1.00 37.04 . 1 789 ATOM O O PRO A 125 . 63.647 −10.250 21.007 1.00 37.81 . 1 790 ATOM C CB PRO A 125 . 61.738 −12.495 19.247 1.00 35.42 . 1 791 ATOM C CG PRO A 125 . 60.303 −12.831 19.055 1.00 34.62 . 1 792 ATOM C CD PRO A 125 . 59.704 −11.488 18.673 1.00 34.84 . 1 793 ATOM N N ASP A 126 . 63.256 −9.842 18.839 1.00 38.18 . 1 794 ATOM C CA ASP A 126 . 64.484 −9.065 18.688 1.00 39.53 . 1 795 ATOM C C ASP A 126 . 64.477 −7.652 19.290 1.00 38.97 . 1 796 ATOM O O ASP A 126 . 65.505 −6.977 19.263 1.00 39.29 . 1 797 ATOM C CB ASP A 126 . 64.859 −8.969 17.204 1.00 42.06 . 1 798 ATOM C CG ASP A 126 . 65.152 −10.328 16.579 1.00 44.71 . 1 799 ATOM O OD1 ASP A 126 . 64.273 −11.225 16.644 1.00 45.73 . 1 800 ATOM O OD2 ASP A 126 . 66.262 −10.493 16.012 1.00 46.29 . 1 801 ATOM N N GLU A 127 . 63.340 −7.207 19.827 1.00 38.01 . 1 802 ATOM C CA GLU A 127 . 63.230 −5.862 20.410 1.00 37.82 . 1 803 ATOM C C GLU A 127 . 64.362 −5.523 21.387 1.00 37.20 . 1 804 ATOM O O GLU A 127 . 64.572 −6.218 22.374 1.00 37.25 . 1 805 ATOM C CB GLU A 127 . 61.876 −5.697 21.109 1.00 37.72 . 1 806 ATOM C CG GLU A 127 . 61.682 −4.370 21.860 1.00 38.37 . 1 807 ATOM C CD GLU A 127 . 62.068 −3.151 21.026 1.00 39.22 . 1 808 ATOM O OE1 GLU A 127 . 61.750 −3.129 19.817 1.00 39.22 . 1 809 ATOM O OE2 GLU A 127 . 62.683 −2.211 21.580 1.00 37.93 . 1 810 ATOM N N SER A 128 . 65.077 −4.438 21.110 1.00 37.05 . 1 811 ATOM C CA SER A 128 . 66.194 −4.023 21.957 1.00 37.35 . 1 812 ATOM C C SER A 128 . 65.786 −3.545 23.351 1.00 36.20 . 1 813 ATOM O O SER A 128 . 66.598 −3.556 24.268 1.00 37.51 . 1 814 ATOM C CB SER A 128 . 67.008 −2.938 21.247 1.00 37.97 . 1 815 ATOM O OG SER A 128 . 66.187 −1.843 20.883 1.00 39.57 . 1 816 ATOM N N ARG A 129 . 64.535 −3.127 23.514 1.00 35.21 . 1 817 ATOM C CA ARG A 129 . 64.050 −2.669 24.809 1.00 34.68 . 1 818 ATOM C C ARG A 129 . 63.671 −3.857 25.697 1.00 34.24 . 1 819 ATOM O O ARG A 129 . 63.535 −3.717 26.913 1.00 33.77 . 1 820 ATOM C CB ARG A 129 . 62.829 −1.765 24.627 1.00 35.15 . 1 821 ATOM C CG ARG A 129 . 63.136 −0.302 24.328 1.00 35.26 . 1 822 ATOM C CD ARG A 129 . 63.444 0.447 25.622 1.00 36.46 . 1 823 ATOM N NE ARG A 129 . 64.849 0.798 25.708 1.00 36.44 . 1 824 ATOM C CZ ARG A 129 . 65.473 1.178 26.818 1.00 36.25 . 1 825 ATOM N NH1 ARG A 129 . 64.820 1.260 27.972 1.00 35.99 . 1 826 ATOM N NH2 ARG A 129 . 66.761 1.471 26.766 1.00 36.01 . 1 827 ATOM N N GLY A 130 . 63.504 −5.024 25.079 1.00 33.37 . 1 828 ATOM C CA GLY A 130 . 63.130 −6.208 25.827 1.00 32.10 . 1 829 ATOM C C GLY A 130 . 61.974 −6.948 25.175 1.00 31.38 . 1 830 ATOM O O GLY A 130 . 61.217 −6.366 24.403 1.00 31.07 . 1 831 ATOM N N TYR A 131 . 61.845 −8.231 25.484 1.00 30.32 . 1 832 ATOM C CA TYR A 131 . 60.786 −9.081 24.932 1.00 29.90 . 1 833 ATOM C C TYR A 131 . 59.972 −9.634 26.095 1.00 28.98 . 1 834 ATOM O O TYR A 131 . 60.538 −10.203 27.023 1.00 29.84 . 1 835 ATOM C CB TYR A 131 . 61.425 −10.230 24.138 1.00 30.88 . 1 836 ATOM C CG TYR A 131 . 60.458 −11.257 23.586 1.00 32.30 . 1 837 ATOM C CD1 TYR A 131 . 59.397 −10.876 22.763 1.00 32.30 . 1 838 ATOM C CD2 TYR A 131 . 60.641 −12.624 23.837 1.00 33.66 . 1 839 ATOM C CE1 TYR A 131 . 58.543 −11.822 22.200 1.00 33.00 . 1 840 ATOM C CE2 TYR A 131 . 59.786 −13.584 23.275 1.00 33.65 . 1 841 ATOM C CZ TYR A 131 . 58.740 −13.170 22.457 1.00 34.05 . 1 842 ATOM O OH TYR A 131 . 57.887 −14.099 21.900 1.00 34.79 . 1 843 ATOM N N LEU A 132 . 58.651 −9.475 26.034 1.00 27.40 . 1 844 ATOM C CA LEU A 132 . 57.754 −9.927 27.088 1.00 26.37 . 1 845 ATOM C C LEU A 132 . 56.687 −10.929 26.651 1.00 26.84 . 1 846 ATOM O O LEU A 132 . 55.944 −11.428 27.488 1.00 27.02 . 1 847 ATOM C CB LEU A 132 . 57.024 −8.724 27.688 1.00 25.81 . 1 848 ATOM C CG LEU A 132 . 57.850 −7.593 28.292 1.00 26.19 . 1 849 ATOM C CD1 LEU A 132 . 56.916 −6.439 28.667 1.00 25.54 . 1 850 ATOM C CD2 LEU A 132 . 58.588 −8.105 29.520 1.00 26.14 . 1 851 ATOM N N ALA A 133 . 56.587 −11.228 25.361 1.00 26.44 . 1 852 ATOM C CA ALA A 133 . 55.536 −12.150 24.919 1.00 27.35 . 1 853 ATOM C C ALA A 133 . 55.657 −13.570 25.472 1.00 27.08 . 1 854 ATOM O O ALA A 133 . 54.651 −14.243 25.676 1.00 26.29 . 1 855 ATOM C CB ALA A 133 . 55.471 −12.189 23.395 1.00 26.76 . 1 856 ATOM N N SER A 134 . 56.878 −14.026 25.712 1.00 28.24 . 1 857 ATOM C CA SER A 134 . 57.074 −15.376 26.233 1.00 29.33 . 1 858 ATOM C C SER A 134 . 56.400 −15.608 27.585 1.00 29.40 . 1 859 ATOM O O SER A 134 . 56.167 −16.751 27.981 1.00 29.50 . 1 860 ATOM C CB SER A 134 . 58.566 −15.700 26.324 1.00 30.86 . 1 861 ATOM O OG SER A 134 . 59.278 −14.667 26.987 1.00 33.12 . 1 862 ATOM N N PHE A 135 . 56.069 −14.538 28.300 1.00 29.54 . 1 863 ATOM C CA PHE A 135 . 55.424 −14.717 29.594 1.00 30.09 . 1 864 ATOM C C PHE A 135 . 53.955 −15.058 29.388 1.00 29.47 . 1 865 ATOM O O PHE A 135 . 53.357 −15.802 30.168 1.00 29.31 . 1 866 ATOM C CB PHE A 135 . 55.568 −13.465 30.470 1.00 32.01 . 1 867 ATOM C CG PHE A 135 . 55.196 −13.698 31.909 1.00 33.69 . 1 868 ATOM C CD1 PHE A 135 . 55.856 −14.666 32.661 1.00 34.38 . 1 869 ATOM C CD2 PHE A 135 . 54.167 −12.982 32.502 1.00 34.50 . 1 870 ATOM C CE1 PHE A 135 . 55.490 −14.917 33.989 1.00 35.01 . 1 871 ATOM C CE2 PHE A 135 . 53.793 −13.225 33.832 1.00 35.06 . 1 872 ATOM C CZ PHE A 135 . 54.460 −14.195 34.570 1.00 34.90 . 1 873 ATOM N N THR A 136 . 53.365 −14.526 28.324 1.00 28.55 . 1 874 ATOM C CA THR A 136 . 51.976 −14.833 28.045 1.00 27.93 . 1 875 ATOM C C THR A 136 . 51.874 −16.314 27.669 1.00 27.90 . 1 876 ATOM O O THR A 136 . 50.920 −16.991 28.033 1.00 26.64 . 1 877 ATOM C CB THR A 136 . 51.430 −13.989 26.873 1.00 27.77 . 1 878 ATOM O OG1 THR A 136 . 51.468 −12.602 27.221 1.00 26.98 . 1 879 ATOM C CG2 THR A 136 . 50.009 −14.384 26.569 1.00 27.13 . 1 880 ATOM N N THR A 137 . 52.862 −16.800 26.930 1.00 28.84 . 1 881 ATOM C CA THR A 137 . 52.872 −18.201 26.510 1.00 30.16 . 1 882 ATOM C C THR A 137 . 52.888 −19.106 27.746 1.00 30.74 . 1 883 ATOM O O THR A 137 . 52.150 −20.084 27.820 1.00 30.90 . 1 884 ATOM C CB THR A 137 . 54.095 −18.480 25.625 1.00 30.56 . 1 885 ATOM O OG1 THR A 137 . 54.125 −17.511 24.565 1.00 30.73 . 1 886 ATOM C CG2 THR A 137 . 54.030 −19.892 25.015 1.00 31.16 . 1 887 ATOM N N PHE A 138 . 53.721 −18.763 28.722 1.00 31.80 . 1 888 ATOM C CA PHE A 138 . 53.800 −19.532 29.960 1.00 32.56 . 1 889 ATOM C C PHE A 138 . 52.445 −19.548 30.663 1.00 33.02 . 1 890 ATOM O O PHE A 138 . 51.925 −20.613 31.014 1.00 32.24 . 1 891 ATOM C CB PHE A 138 . 54.861 −18.925 30.887 1.00 33.64 . 1 892 ATOM C CG PHE A 138 . 54.820 −19.463 32.295 1.00 35.25 . 1 893 ATOM C CD1 PHE A 138 . 55.084 −20.805 32.548 1.00 36.07 . 1 894 ATOM C CD2 PHE A 138 . 54.481 −18.631 33.360 1.00 35.85 . 1 895 ATOM C CE1 PHE A 138 . 55.008 −21.317 33.845 1.00 37.19 . 1 896 ATOM C CE2 PHE A 138 . 54.402 −19.128 34.663 1.00 36.55 . 1 897 ATOM C CZ PHE A 138 . 54.666 −20.476 34.904 1.00 36.91 . 1 898 ATOM N N LEU A 139 . 51.857 −18.368 30.857 1.00 32.71 . 1 899 ATOM C CA LEU A 139 . 50.570 −18.273 31.539 1.00 33.47 . 1 900 ATOM C C LEU A 139 . 49.477 −19.080 30.855 1.00 33.44 . 1 901 ATOM O O LEU A 139 . 48.628 −19.680 31.518 1.00 32.61 . 1 902 ATOM C CB LEU A 139 . 50.127 −16.805 31.654 1.00 33.04 . 1 903 ATOM C CG LEU A 139 . 51.027 −15.932 32.530 1.00 34.00 . 1 904 ATOM C CD1 LEU A 139 . 50.448 −14.517 32.639 1.00 34.11 . 1 905 ATOM C CD2 LEU A 139 . 51.139 −16.566 33.921 1.00 34.10 . 1 906 ATOM N N CYS A 140 . 49.495 −19.084 29.528 1.00 34.99 . 1 907 ATOM C CA CYS A 140 . 48.499 −19.809 28.754 1.00 36.81 . 1 908 ATOM C C CYS A 140 . 48.812 −21.297 28.578 1.00 38.14 . 1 909 ATOM O O CYS A 140 . 48.070 −22.014 27.909 1.00 38.32 . 1 910 ATOM C CB CYS A 140 . 48.325 −19.148 27.382 1.00 36.11 . 1 911 ATOM S SG CYS A 140 . 47.418 −17.571 27.427 1.00 38.46 . 1 912 ATOM N N TYR A 141 . 49.900 −21.766 29.177 1.00 39.88 . 1 913 ATOM C CA TYR A 141 . 50.261 −23.179 29.070 1.00 41.77 . 1 914 ATOM C C TYR A 141 . 49.108 −24.035 29.607 1.00 43.00 . 1 915 ATOM O O TYR A 141 . 48.591 −23.786 30.696 1.00 43.07 . 1 916 ATOM C CB TYR A 141 . 51.527 −23.469 29.873 1.00 42.49 . 1 917 ATOM C CG TYR A 141 . 52.147 −24.812 29.558 1.00 43.46 . 1 918 ATOM C CD1 TYR A 141 . 52.878 −25.003 28.385 1.00 44.29 . 1 919 ATOM C CD2 TYR A 141 . 51.979 −25.900 30.416 1.00 44.33 . 1 920 ATOM C CE1 TYR A 141 . 53.430 −26.247 28.072 1.00 44.99 . 1 921 ATOM C CE2 TYR A 141 . 52.526 −27.153 30.112 1.00 44.58 . 1 922 ATOM C CZ TYR A 141 . 53.249 −27.318 28.940 1.00 44.77 . 1 923 ATOM O OH TYR A 141 . 53.795 −28.545 28.636 1.00 44.52 . 1 924 ATOM N N PRO A 142 . 48.695 −25.063 28.845 1.00 44.33 . 1 925 ATOM C CA PRO A 142 . 47.601 −25.967 29.222 1.00 44.95 . 1 926 ATOM C C PRO A 142 . 47.566 −26.398 30.692 1.00 45.39 . 1 927 ATOM O O PRO A 142 . 46.532 −26.297 31.348 1.00 45.44 . 1 928 ATOM C CB PRO A 142 . 47.796 −27.144 28.273 1.00 45.19 . 1 929 ATOM C CG PRO A 142 . 48.294 −26.470 27.032 1.00 44.92 . 1 930 ATOM C CD PRO A 142 . 49.321 −25.504 27.584 1.00 44.44 . 1 931 ATOM N N ALA A 143 . 48.691 −26.877 31.208 1.00 46.20 . 1 932 ATOM C CA ALA A 143 . 48.755 −27.318 32.598 1.00 47.02 . 1 933 ATOM C C ALA A 143 . 48.338 −26.234 33.602 1.00 47.69 . 1 934 ATOM O O ALA A 143 . 47.801 −26.541 34.664 1.00 48.26 . 1 935 ATOM C CB ALA A 143 . 50.163 −27.814 32.923 1.00 46.87 . 1 936 ATOM N N LEU A 144 . 48.581 −24.971 33.272 1.00 48.22 . 1 937 ATOM C CA LEU A 144 . 48.226 −23.882 34.179 1.00 48.65 . 1 938 ATOM C C LEU A 144 . 46.788 −23.396 34.042 1.00 48.91 . 1 939 ATOM O O LEU A 144 . 46.213 −22.872 34.997 1.00 48.95 . 1 940 ATOM C CB LEU A 144 . 49.180 −22.704 33.987 1.00 48.76 . 1 941 ATOM C CG LEU A 144 . 50.618 −22.950 34.439 1.00 49.15 . 1 942 ATOM C CD1 LEU A 144 . 51.458 −21.718 34.174 1.00 49.17 . 1 943 ATOM C CD2 LEU A 144 . 50.625 −23.297 35.924 1.00 49.61 . 1 944 ATOM N N LEU A 145 . 46.207 −23.574 32.861 1.00 49.10 . 1 945 ATOM C CA LEU A 145 . 44.836 −23.141 32.621 1.00 49.55 . 1 946 ATOM C C LEU A 145 . 43.843 −23.723 33.618 1.00 49.65 . 1 947 ATOM O O LEU A 145 . 42.956 −23.017 34.102 1.00 49.23 . 1 948 ATOM C CB LEU A 145 . 44.409 −23.495 31.195 1.00 49.62 . 1 949 ATOM C CG LEU A 145 . 44.517 −22.349 30.186 1.00 49.97 . 1 950 ATOM C CD1 LEU A 145 . 43.488 −21.278 30.523 1.00 50.24 . 1 951 ATOM C CD2 LEU A 145 . 45.918 −21.767 30.207 1.00 50.35 . 1 952 ATOM N N GLN A 146 . 43.987 −25.009 33.925 1.00 49.55 . 1 953 ATOM C CA GLN A 146 . 43.084 −25.643 34.873 1.00 49.45 . 1 954 ATOM C C GLN A 146 . 43.347 −25.112 36.269 1.00 48.41 . 1 955 ATOM O O GLN A 146 . 42.486 −25.188 37.143 1.00 48.68 . 1 956 ATOM C CB GLN A 146 . 43.233 −27.170 34.832 1.00 51.04 . 1 957 ATOM C CG GLN A 146 . 42.438 −27.826 33.694 1.00 52.20 . 1 958 ATOM C CD GLN A 146 . 40.924 −27.753 33.902 1.00 52.97 . 1 959 ATOM O OE1 GLN A 146 . 40.354 −28.513 34.689 1.00 53.41 . 1 960 ATOM N NE2 GLN A 146 . 40.272 −26.829 33.201 1.00 52.77 . 1 961 ATOM N N VAL A 147 . 44.537 −24.565 36.480 1.00 46.89 . 1 962 ATOM C CA VAL A 147 . 44.865 −23.998 37.775 1.00 45.43 . 1 963 ATOM C C VAL A 147 . 44.183 −22.633 37.880 1.00 44.77 . 1 964 ATOM O O VAL A 147 . 43.593 −22.303 38.911 1.00 43.44 . 1 965 ATOM C CB VAL A 147 . 46.385 −23.835 37.940 1.00 45.32 . 1 966 ATOM C CG1 VAL A 147 . 46.694 −23.013 39.178 1.00 45.51 . 1 967 ATOM C CG2 VAL A 147 . 47.037 −25.204 38.059 1.00 45.51 . 1 968 ATOM N N TRP A 148 . 44.248 −21.856 36.798 1.00 44.05 . 1 969 ATOM C CA TRP A 148 . 43.642 −20.525 36.764 1.00 44.04 . 1 970 ATOM C C TRP A 148 . 42.155 −20.568 37.044 1.00 43.74 . 1 971 ATOM O O TRP A 148 . 41.657 −19.871 37.926 1.00 44.10 . 1 972 ATOM C CB TRP A 148 . 43.835 −19.874 35.397 1.00 43.88 . 1 973 ATOM C CG TRP A 148 . 45.242 −19.707 34.993 1.00 44.01 . 1 974 ATOM C CD1 TRP A 148 . 45.758 −19.907 33.750 1.00 44.17 . 1 975 ATOM C CD2 TRP A 148 . 46.328 −19.298 35.820 1.00 44.38 . 1 976 ATOM N NE1 TRP A 148 . 47.104 −19.650 33.750 1.00 44.49 . 1 977 ATOM C CE2 TRP A 148 . 47.481 −19.275 35.008 1.00 44.26 . 1 978 ATOM C CE3 TRP A 148 . 46.443 −18.952 37.172 1.00 45.05 . 1 979 ATOM C CZ2 TRP A 148 . 48.734 −18.915 35.501 1.00 45.32 . 1 980 ATOM C CZ3 TRP A 148 . 47.687 −18.595 37.662 1.00 45.89 . 1 981 ATOM C CH2 TRP A 148 . 48.818 −18.581 36.828 1.00 46.20 . 1 982 HETA N N MSE A 149 . 41.451 −21.389 36.275 1.00 43.63 . 1 983 HETA C CA MSE A 149 . 40.011 −21.505 36.403 1.00 43.82 . 1 984 HETA C C MSE A 149 . 39.526 −22.131 37.706 1.00 43.46 . 1 985 HETA O O MSE A 149 . 38.326 −22.198 37.953 1.00 43.55 . 1 986 HETA C CB MSE A 149 . 39.459 −22.258 35.198 1.00 44.79 . 1 987 HETA C CG MSE A 149 . 39.694 −21.519 33.879 1.00 46.41 . 1 988 HETA SE SE MSE A 149 . 38.956 −19.859 33.826 1.00 47.37 . 1 989 HETA C CE MSE A 149 . 40.336 −18.829 34.213 1.00 47.87 . 1 990 ATOM N N ASN A 150 . 40.454 −22.587 38.538 1.00 43.32 . 1 991 ATOM C CA ASN A 150 . 40.094 −23.167 39.829 1.00 43.32 . 1 992 ATOM C C ASN A 150 . 40.673 −22.283 40.932 1.00 42.93 . 1 993 ATOM O O ASN A 150 . 40.856 −22.709 42.074 1.00 41.78 . 1 994 ATOM C CB ASN A 150 . 40.642 −24.589 39.945 1.00 44.51 . 1 995 ATOM C CG ASN A 150 . 39.888 −25.574 39.076 1.00 45.90 . 1 996 ATOM O OD1 ASN A 150 . 38.676 −25.737 39.217 1.00 47.24 . 1 997 ATOM N ND2 ASN A 150 . 40.599 −26.237 38.173 1.00 46.05 . 1 998 ATOM N N PHE A 151 . 40.955 −21.039 40.563 1.00 42.64 . 1 999 ATOM C CA PHE A 151 . 41.526 −20.056 41.471 1.00 43.11 . 1 1000 ATOM C C PHE A 151 . 40.882 −20.059 42.859 1.00 43.61 . 1 1001 ATOM O O PHE A 151 . 41.580 −19.980 43.869 1.00 44.21 . 1 1002 ATOM C CB PHE A 151 . 41.399 −18.661 40.856 1.00 42.33 . 1 1003 ATOM C CG PHE A 151 . 42.267 −17.633 41.508 1.00 41.28 . 1 1004 ATOM C CD1 PHE A 151 . 43.594 −17.487 41.129 1.00 41.26 . 1 1005 ATOM C CD2 PHE A 151 . 41.766 −16.822 42.518 1.00 41.31 . 1 1006 ATOM C CE1 PHE A 151 . 44.411 −16.546 41.746 1.00 40.92 . 1 1007 ATOM C CE2 PHE A 151 . 42.575 −15.881 43.142 1.00 40.50 . 1 1008 ATOM C CZ PHE A 151 . 43.900 −15.742 42.754 1.00 40.25 . 1 1009 ATOM N N LYS A 152 . 39.558 −20.155 42.909 1.00 44.74 . 1 1010 ATOM C CA LYS A 152 . 38.839 −20.149 44.182 1.00 46.18 . 1 1011 ATOM C C LYS A 152 . 39.316 −21.191 45.196 1.00 46.81 . 1 1012 ATOM O O LYS A 152 . 39.140 −21.008 46.396 1.00 46.69 . 1 1013 ATOM C CB LYS A 152 . 37.336 −20.342 43.956 1.00 46.38 . 1 1014 ATOM C CG LYS A 152 . 36.957 −21.701 43.389 1.00 47.19 . 1 1015 ATOM C CD LYS A 152 . 35.481 −21.999 43.608 1.00 48.24 . 1 1016 ATOM C CE LYS A 152 . 35.165 −22.092 45.099 1.00 49.40 . 1 1017 ATOM N NZ LYS A 152 . 33.725 −22.366 45.384 1.00 50.15 . 1 1018 ATOM N N GLU A 153 . 39.914 −22.277 44.719 1.00 48.04 . 1 1019 ATOM C CA GLU A 153 . 40.395 −23.333 45.610 1.00 49.71 . 1 1020 ATOM C C GLU A 153 . 41.478 −22.852 46.571 1.00 50.04 . 1 1021 ATOM O O GLU A 153 . 41.369 −23.028 47.785 1.00 50.48 . 1 1022 ATOM C CB GLU A 153 . 40.948 −24.508 44.804 1.00 50.40 . 1 1023 ATOM C CG GLU A 153 . 40.004 −25.066 43.757 1.00 52.64 . 1 1024 ATOM C CD GLU A 153 . 38.580 −25.206 44.255 1.00 54.00 . 1 1025 ATOM O OE1 GLU A 153 . 38.382 −25.666 45.401 1.00 55.41 . 1 1026 ATOM O OE2 GLU A 153 . 37.655 −24.862 43.488 1.00 55.02 . 1 1027 ATOM N N ALA A 154 . 42.528 −22.256 46.020 1.00 50.72 . 1 1028 ATOM C CA ALA A 154 . 43.638 −21.760 46.825 1.00 51.38 . 1 1029 ATOM C C ALA A 154 . 43.192 −20.717 47.843 1.00 52.20 . 1 1030 ATOM O O ALA A 154 . 43.817 −20.555 48.893 1.00 51.92 . 1 1031 ATOM C CB ALA A 154 . 44.712 −21.177 45.920 1.00 50.81 . 1 1032 ATOM N N VAL A 155 . 42.110 −20.012 47.534 1.00 53.16 . 1 1033 ATOM C CA VAL A 155 . 41.603 −18.987 48.434 1.00 54.80 . 1 1034 ATOM C C VAL A 155 . 40.896 −19.575 49.655 1.00 56.22 . 1 1035 ATOM O O VAL A 155 . 41.202 −19.209 50.787 1.00 56.04 . 1 1036 ATOM C CB VAL A 155 . 40.628 −18.028 47.695 1.00 54.51 . 1 1037 ATOM C CG1 VAL A 155 . 39.913 −17.123 48.687 1.00 54.40 . 1 1038 ATOM C CG2 VAL A 155 . 41.399 −17.176 46.698 1.00 54.29 . 1 1039 ATOM N N VAL A 156 . 39.967 −20.496 49.425 1.00 58.16 . 1 1040 ATOM C CA VAL A 156 . 39.209 −21.093 50.518 1.00 60.64 . 1 1041 ATOM C C VAL A 156 . 39.953 −22.127 51.362 1.00 62.57 . 1 1042 ATOM O O VAL A 156 . 39.552 −22.410 52.493 1.00 62.54 . 1 1043 ATOM C CB VAL A 156 . 37.908 −21.731 49.994 1.00 60.42 . 1 1044 ATOM C CG1 VAL A 156 . 37.010 −20.655 49.417 1.00 60.67 . 1 1045 ATOM C CG2 VAL A 156 . 38.224 −22.777 48.934 1.00 60.79 . 1 1046 ATOM N N ASP A 157 . 41.036 −22.681 50.828 1.00 64.88 . 1 1047 ATOM C CA ASP A 157 . 41.797 −23.690 51.555 1.00 67.33 . 1 1048 ATOM C C ASP A 157 . 43.183 −23.234 51.974 1.00 68.63 . 1 1049 ATOM O O ASP A 157 . 43.996 −22.838 51.141 1.00 69.04 . 1 1050 ATOM C CB ASP A 157 . 41.916 −24.959 50.712 1.00 68.06 . 1 1051 ATOM C CG ASP A 157 . 40.568 −25.543 50.356 1.00 69.25 . 1 1052 ATOM O OD1 ASP A 157 . 39.782 −25.828 51.287 1.00 70.17 . 1 1053 ATOM O OD2 ASP A 157 . 40.291 −25.717 49.150 1.00 70.04 . 1 1054 ATOM N N GLU A 158 . 43.452 −23.298 53.273 1.00 70.12 . 1 1055 ATOM C CA GLU A 158 . 44.750 −22.907 53.803 1.00 71.60 . 1 1056 ATOM C C GLU A 158 . 45.756 −24.000 53.449 1.00 72.41 . 1 1057 ATOM O O GLU A 158 . 46.798 −24.142 54.085 1.00 72.66 . 1 1058 ATOM C CB GLU A 158 . 44.660 −22.727 55.322 1.00 71.77 . 1 1059 ATOM C CG GLU A 158 . 45.929 −22.203 55.971 1.00 72.59 . 1 1060 ATOM C CD GLU A 158 . 45.705 −21.747 57.401 1.00 72.99 . 1 1061 ATOM O OE1 GLU A 158 . 45.124 −22.523 58.191 1.00 73.25 . 1 1062 ATOM O OE2 GLU A 158 . 46.112 −20.613 57.734 1.00 72.94 . 1 1063 ATOM N N ASP A 159 . 45.422 −24.765 52.414 1.00 73.44 . 1 1064 ATOM C CA ASP A 159 . 46.252 −25.861 51.925 1.00 74.36 . 1 1065 ATOM C C ASP A 159 . 47.640 −25.362 51.533 1.00 74.65 . 1 1066 ATOM O O ASP A 159 . 48.538 −25.273 52.371 1.00 38.85 . 1 1067 ATOM C CB ASP A 159 . 45.582 −26.510 50.711 1.00 75.13 . 1 1068 ATOM C CG ASP A 159 . 45.809 −28.009 50.647 1.00 76.13 . 1 1069 ATOM O OD1 ASP A 159 . 46.980 −28.444 50.697 1.00 76.90 . 1 1070 ATOM O OD2 ASP A 159 . 44.812 −28.755 50.543 1.00 76.36 . 1 1071 ATOM N N LYS A 180 . 26.121 −28.429 33.961 1.00 42.15 . 1 1072 ATOM C CA LYS A 180 . 25.854 −28.676 32.520 1.00 41.98 . 1 1073 ATOM C C LYS A 180 . 26.050 −27.399 31.708 1.00 41.80 . 1 1074 ATOM O O LYS A 180 . 25.502 −26.338 32.021 1.00 41.43 . 1 1075 ATOM C CB LYS A 180 . 24.434 −29.209 32.330 1.00 42.48 . 1 1076 ATOM C CG LYS A 180 . 24.220 −29.888 30.994 1.00 43.75 . 1 1077 ATOM C CD LYS A 180 . 23.013 −30.822 31.012 1.00 44.26 . 1 1078 ATOM C CE LYS A 180 . 23.006 −31.702 29.769 1.00 45.35 . 1 1079 ATOM N NZ LYS A 180 . 21.911 −32.721 29.766 1.00 45.35 . 1 1080 HETA N N MSE A 181 . 26.846 −27.524 30.659 1.00 41.58 . 1 1081 HETA C CA MSE A 181 . 27.167 −26.423 29.773 1.00 41.22 . 1 1082 HETA C C MSE A 181 . 25.903 −25.770 29.220 1.00 40.83 . 1 1083 HETA O O MSE A 181 . 25.789 −24.548 29.174 1.00 40.46 . 1 1084 HETA C CB MSE A 181 . 28.026 −26.957 28.632 1.00 41.38 . 1 1085 HETA C CG MSE A 181 . 28.813 −25.917 27.879 1.00 41.80 . 1 1086 HETA SE SE MSE A 181 . 29.760 −26.700 26.580 1.00 41.32 . 1 1087 HETA C CE MSE A 181 . 29.463 −25.566 25.230 1.00 41.73 . 1 1088 ATOM N N ASN A 182 . 24.948 −26.595 28.808 1.00 40.16 . 1 1089 ATOM C CA ASN A 182 . 23.709 −26.093 28.241 1.00 39.84 . 1 1090 ATOM C C ASN A 182 . 22.982 −25.126 29.176 1.00 39.12 . 1 1091 ATOM O O ASN A 182 . 22.519 −24.070 28.744 1.00 38.48 . 1 1092 ATOM C CB ASN A 182 . 22.792 −27.265 27.870 1.00 40.95 . 1 1093 ATOM C CG ASN A 182 . 21.542 −26.817 27.135 1.00 42.25 . 1 1094 ATOM O OD1 ASN A 182 . 20.438 −26.813 27.697 1.00 42.76 . 1 1095 ATOM N ND2 ASN A 182 . 21.708 −26.427 25.872 1.00 42.00 . 1 1096 ATOM N N GLN A 183 . 22.884 −25.486 30.452 1.00 38.14 . 1 1097 ATOM C CA GLN A 183 . 22.205 −24.645 31.431 1.00 37.85 . 1 1098 ATOM C C GLN A 183 . 22.912 −23.318 31.672 1.00 37.00 . 1 1099 ATOM O O GLN A 183 . 22.264 −22.294 31.856 1.00 35.67 . 1 1100 ATOM C CB GLN A 183 . 22.076 −25.376 32.769 1.00 38.92 . 1 1101 ATOM C CG GLN A 183 . 21.507 −24.509 33.888 1.00 40.24 . 1 1102 ATOM C CD GLN A 183 . 22.548 −24.131 34.939 1.00 41.93 . 1 1103 ATOM O OE1 GLN A 183 . 23.576 −23.527 34.633 1.00 42.78 . 1 1104 ATOM N NE2 GLN A 183 . 22.279 −24.492 36.189 1.00 43.09 . 1 1105 ATOM N N ILE A 184 . 24.239 −23.356 31.701 1.00 36.43 . 1 1106 ATOM C CA ILE A 184 . 25.032 −22.164 31.932 1.00 37.01 . 1 1107 ATOM C C ILE A 184 . 24.914 −21.216 30.740 1.00 37.28 . 1 1108 ATOM O O ILE A 184 . 24.819 −20.005 30.918 1.00 36.80 . 1 1109 ATOM C CB ILE A 184 . 26.510 −22.539 32.177 1.00 37.00 . 1 1110 ATOM C CG1 ILE A 184 . 26.628 −23.300 33.503 1.00 37.55 . 1 1111 ATOM C CG2 ILE A 184 . 27.377 −21.290 32.226 1.00 36.97 . 1 1112 ATOM C CD1 ILE A 184 . 28.025 −23.821 33.794 1.00 38.25 . 1 1113 ATOM N N PHE A 185 . 24.903 −21.771 29.530 1.00 37.02 . 1 1114 ATOM C CA PHE A 185 . 24.781 −20.956 28.326 1.00 36.80 . 1 1115 ATOM C C PHE A 185 . 23.427 −20.275 28.275 1.00 37.06 . 1 1116 ATOM O O PHE A 185 . 23.335 −19.056 28.104 1.00 35.96 . 1 1117 ATOM C CB PHE A 185 . 24.945 −21.810 27.066 1.00 37.75 . 1 1118 ATOM C CG PHE A 185 . 24.752 −21.040 25.789 1.00 38.11 . 1 1119 ATOM C CD1 PHE A 185 . 25.657 −20.046 25.418 1.00 38.92 . 1 1120 ATOM C CD2 PHE A 185 . 23.654 −21.285 24.970 1.00 38.72 . 1 1121 ATOM C CE1 PHE A 185 . 25.471 −19.306 24.250 1.00 38.48 . 1 1122 ATOM C CE2 PHE A 185 . 23.458 −20.550 23.798 1.00 38.86 . 1 1123 ATOM C CZ PHE A 185 . 24.371 −19.560 23.440 1.00 38.69 . 1 1124 ATOM N N ASN A 186 . 22.373 −21.071 28.419 1.00 36.83 . 1 1125 ATOM C CA ASN A 186 . 21.021 −20.549 28.370 1.00 37.14 . 1 1126 ATOM C C ASN A 186 . 20.771 −19.526 29.455 1.00 36.83 . 1 1127 ATOM O O ASN A 186 . 20.000 −18.588 29.257 1.00 36.59 . 1 1128 ATOM C CB ASN A 186 . 20.001 −21.681 28.494 1.00 38.05 . 1 1129 ATOM C CG ASN A 186 . 20.175 −22.730 27.419 1.00 39.77 . 1 1130 ATOM O OD1 ASN A 186 . 20.474 −22.406 26.266 1.00 40.08 . 1 1131 ATOM N ND2 ASN A 186 . 19.986 −23.996 27.786 1.00 40.19 . 1 1132 ATOM N N LYS A 187 . 21.412 −19.712 30.603 1.00 35.89 . 1 1133 ATOM C CA LYS A 187 . 21.236 −18.788 31.707 1.00 36.11 . 1 1134 ATOM C C LYS A 187 . 21.899 −17.453 31.369 1.00 35.48 . 1 1135 ATOM O O LYS A 187 . 21.296 −16.394 31.545 1.00 34.84 . 1 1136 ATOM C CB LYS A 187 . 21.847 −19.360 32.984 1.00 37.15 . 1 1137 ATOM C CG LYS A 187 . 21.269 −18.761 34.253 1.00 39.84 . 1 1138 ATOM C CD LYS A 187 . 21.998 −19.290 35.483 1.00 42.71 . 1 1139 ATOM C CE LYS A 187 . 21.072 −19.397 36.700 1.00 44.41 . 1 1140 ATOM N NZ LYS A 187 . 20.110 −20.544 36.596 1.00 45.04 . 1 1141 ATOM N N SER A 188 . 23.135 −17.508 30.884 1.00 34.86 . 1 1142 ATOM C CA SER A 188 . 23.845 −16.287 30.523 1.00 35.62 . 1 1143 ATOM C C SER A 188 . 23.127 −15.537 29.390 1.00 35.03 . 1 1144 ATOM O O SER A 188 . 23.041 −14.307 29.397 1.00 33.71 . 1 1145 ATOM C CB SER A 188 . 25.291 −16.610 30.122 1.00 35.72 . 1 1146 ATOM O OG SER A 188 . 25.353 −17.439 28.977 1.00 38.00 . 1 1147 HETA N N MSE A 189 . 22.602 −16.275 28.418 1.00 34.64 . 1 1148 HETA C CA MSE A 189 . 21.897 −15.640 27.312 1.00 34.19 . 1 1149 HETA C C MSE A 189 . 20.631 −14.926 27.781 1.00 33.83 . 1 1150 HETA O O MSE A 189 . 20.301 −13.841 27.295 1.00 33.03 . 1 1151 HETA C CB MSE A 189 . 21.568 −16.674 26.235 1.00 34.52 . 1 1152 HETA C CG MSE A 189 . 22.784 −17.109 25.441 1.00 34.99 . 1 1153 HETA SE SE MSE A 189 . 23.580 −15.747 24.541 1.00 36.38 . 1 1154 HETA C CE MSE A 189 . 25.101 −15.590 25.416 1.00 35.33 . 1 1155 ATOM N N VAL A 190 . 19.923 −15.522 28.735 1.00 33.60 . 1 1156 ATOM C CA VAL A 190 . 18.714 −14.903 29.256 1.00 33.47 . 1 1157 ATOM C C VAL A 190 . 19.048 −13.630 30.043 1.00 33.43 . 1 1158 ATOM O O VAL A 190 . 18.335 −12.625 29.948 1.00 33.20 . 1 1159 ATOM C CB VAL A 190 . 17.932 −15.878 30.173 1.00 33.43 . 1 1160 ATOM C CG1 VAL A 190 . 16.929 −15.116 31.024 1.00 33.63 . 1 1161 ATOM C CG2 VAL A 190 . 17.191 −16.902 29.323 1.00 34.51 . 1 1162 ATOM N N ASP A 191 . 20.129 −13.682 30.818 1.00 32.69 . 1 1163 ATOM C CA ASP A 191 . 20.551 −12.542 31.629 1.00 32.38 . 1 1164 ATOM C C ASP A 191 . 21.022 −11.351 30.798 1.00 31.68 . 1 1165 ATOM O O ASP A 191 . 20.595 −10.225 31.031 1.00 30.91 . 1 1166 ATOM C CB ASP A 191 . 21.666 −12.957 32.588 1.00 32.78 . 1 1167 ATOM C CG ASP A 191 . 21.208 −13.974 33.610 1.00 33.69 . 1 1168 ATOM O OD1 ASP A 191 . 20.017 −13.955 33.992 1.00 33.53 . 1 1169 ATOM O OD2 ASP A 191 . 22.054 −14.782 34.047 1.00 35.18 . 1 1170 ATOM N N VAL A 192 . 21.915 −11.597 29.847 1.00 31.29 . 1 1171 ATOM C CA VAL A 192 . 22.411 −10.526 28.988 1.00 32.31 . 1 1172 ATOM C C VAL A 192 . 21.246 −9.912 28.195 1.00 32.73 . 1 1173 ATOM O O VAL A 192 . 21.180 −8.690 28.008 1.00 32.04 . 1 1174 ATOM C CB VAL A 192 . 23.497 −11.055 28.020 1.00 32.51 . 1 1175 ATOM C CG1 VAL A 192 . 23.877 −9.983 27.010 1.00 32.36 . 1 1176 ATOM C CG2 VAL A 192 . 24.728 −11.472 28.811 1.00 33.04 . 1 1177 ATOM N N CYS A 193 . 20.321 −10.765 27.750 1.00 32.85 . 1 1178 ATOM C CA CYS A 193 . 19.152 −10.319 26.997 1.00 32.70 . 1 1179 ATOM C C CYS A 193 . 18.262 −9.382 27.789 1.00 32.44 . 1 1180 ATOM O O CYS A 193 . 17.780 −8.370 27.268 1.00 31.66 . 1 1181 ATOM C CB CYS A 193 . 18.313 −11.509 26.560 1.00 34.55 . 1 1182 ATOM S SG CYS A 193 . 18.481 −11.878 24.835 1.00 39.78 . 1 1183 ATOM N N ALA A 194 . 18.021 −9.729 29.047 1.00 31.11 . 1 1184 ATOM C CA ALA A 194 . 17.182 −8.903 29.899 1.00 30.88 . 1 1185 ATOM C C ALA A 194 . 17.851 −7.546 30.100 1.00 30.75 . 1 1186 ATOM O O ALA A 194 . 17.175 −6.519 30.149 1.00 30.18 . 1 1187 ATOM C CB ALA A 194 . 16.955 −9.587 31.249 1.00 30.48 . 1 1188 ATOM N N THR A 195 . 19.176 −7.553 30.212 1.00 30.23 . 1 1189 ATOM C CA THR A 195 . 19.938 −6.321 30.411 1.00 30.35 . 1 1190 ATOM C C THR A 195 . 19.845 −5.423 29.162 1.00 30.59 . 1 1191 ATOM O O THR A 195 . 19.549 −4.230 29.260 1.00 29.89 . 1 1192 ATOM C CB THR A 195 . 21.418 −6.648 30.732 1.00 30.32 . 1 1193 ATOM O OG1 THR A 195 . 21.478 −7.498 31.899 1.00 30.01 . 1 1194 ATOM C CG2 THR A 195 . 22.204 −5.370 31.004 1.00 29.70 . 1 1195 ATOM N N GLU A 196 . 20.080 −6.003 27.990 1.00 30.28 . 1 1196 ATOM C CA GLU A 196 . 20.001 −5.249 26.740 1.00 30.85 . 1 1197 ATOM C C GLU A 196 . 18.601 −4.683 26.491 1.00 30.86 . 1 1198 ATOM O O GLU A 196 . 18.443 −3.504 26.169 1.00 30.77 . 1 1199 ATOM C CB GLU A 196 . 20.404 −6.137 25.560 1.00 30.25 . 1 1200 ATOM C CG GLU A 196 . 21.854 −6.585 25.600 1.00 31.91 . 1 1201 ATOM C CD GLU A 196 . 22.151 −7.676 24.595 1.00 32.32 . 1 1202 ATOM O OE1 GLU A 196 . 21.293 −8.562 24.418 1.00 33.21 . 1 1203 ATOM O OE2 GLU A 196 . 23.244 −7.659 23.998 1.00 34.27 . 1 1204 HETA N N MSE A 197 . 17.585 −5.524 26.655 1.00 30.89 . 1 1205 HETA C CA MSE A 197 . 16.206 −5.119 26.426 1.00 30.65 . 1 1206 HETA C C MSE A 197 . 15.681 −4.058 27.392 1.00 31.59 . 1 1207 HETA O O MSE A 197 . 14.875 −3.201 27.002 1.00 31.69 . 1 1208 HETA C CB MSE A 197 . 15.294 −6.345 26.459 1.00 30.46 . 1 1209 HETA C CG MSE A 197 . 15.529 −7.345 25.324 1.00 29.75 . 1 1210 HETA SE SE MSE A 197 . 15.112 −6.701 23.669 1.00 29.38 . 1 1211 HETA C CE MSE A 197 . 13.536 −6.071 23.981 1.00 27.63 . 1 1212 ATOM N N LYS A 198 . 16.115 −4.102 28.650 1.00 31.69 . 1 1213 ATOM C CA LYS A 198 . 15.647 −3.101 29.597 1.00 32.51 . 1 1214 ATOM C C LYS A 198 . 16.034 −1.715 29.070 1.00 32.33 . 1 1215 ATOM O O LYS A 198 . 15.204 −0.809 29.001 1.00 32.72 . 1 1216 ATOM C CB LYS A 198 . 16.265 −3.318 30.981 1.00 32.71 . 1 1217 ATOM C CG LYS A 198 . 15.725 −2.357 32.031 1.00 33.78 . 1 1218 ATOM C CD LYS A 198 . 16.365 −2.562 33.387 1.00 34.43 . 1 1219 ATOM C CE LYS A 198 . 15.945 −1.461 34.351 1.00 34.87 . 1 1220 ATOM N NZ LYS A 198 . 14.479 −1.435 34.601 1.00 34.60 . 1 1221 ATOM N N ARG A 199 . 17.295 −1.576 28.680 1.00 32.51 . 1 1222 ATOM C CA ARG A 199 . 17.825 −0.318 28.164 1.00 34.13 . 1 1223 ATOM C C ARG A 199 . 17.159 0.102 26.841 1.00 35.17 . 1 1224 ATOM O O ARG A 199 . 16.705 1.237 26.706 1.00 35.40 . 1 1225 ATOM C CB ARG A 199 . 19.336 −0.451 27.981 1.00 33.24 . 1 1226 ATOM C CG ARG A 199 . 20.039 0.744 27.367 1.00 33.82 . 1 1227 ATOM C CD ARG A 199 . 20.359 1.852 28.359 1.00 34.16 . 1 1228 ATOM N NE ARG A 199 . 19.199 2.651 28.730 1.00 34.77 . 1 1229 ATOM C CZ ARG A 199 . 19.184 3.984 28.759 1.00 34.52 . 1 1230 ATOM N NH1 ARG A 199 . 20.263 4.670 28.432 1.00 35.89 . 1 1231 ATOM N NH2 ARG A 199 . 18.093 4.629 29.145 1.00 33.89 . 1 1232 HETA N N MSE A 200 . 17.099 −0.812 25.874 1.00 36.26 . 1 1233 HETA C CA MSE A 200 . 16.486 −0.504 24.582 1.00 37.06 . 1 1234 HETA C C MSE A 200 . 15.099 0.098 24.756 1.00 36.89 . 1 1235 HETA O O MSE A 200 . 14.806 1.168 24.211 1.00 36.61 . 1 1236 HETA C CB MSE A 200 . 16.362 −1.758 23.713 1.00 39.08 . 1 1237 HETA C CG MSE A 200 . 15.794 −1.467 22.312 1.00 41.08 . 1 1238 HETA SE SE MSE A 200 . 14.603 −2.707 21.714 1.00 44.48 . 1 1239 HETA C CE MSE A 200 . 15.653 −3.982 21.269 1.00 39.65 . 1 1240 ATOM N N LEU A 201 . 14.245 −0.586 25.512 1.00 36.03 . 1 1241 ATOM C CA LEU A 201 . 12.891 −0.104 25.734 1.00 35.99 . 1 1242 ATOM C C LEU A 201 . 12.811 1.303 26.327 1.00 36.09 . 1 1243 ATOM O O LEU A 201 . 11.820 2.002 26.127 1.00 35.59 . 1 1244 ATOM C CB LEU A 201 . 12.112 −1.080 26.623 1.00 36.80 . 1 1245 ATOM C CG LEU A 201 . 11.789 −2.446 26.005 1.00 36.70 . 1 1246 ATOM C CD1 LEU A 201 . 10.928 −3.243 26.971 1.00 37.69 . 1 1247 ATOM C CD2 LEU A 201 . 11.066 −2.263 24.685 1.00 37.52 . 1 1248 ATOM N N GLU A 202 . 13.844 1.724 27.049 1.00 35.98 . 1 1249 ATOM C CA GLU A 202 . 13.833 3.056 27.640 1.00 36.79 . 1 1250 ATOM C C GLU A 202 . 14.169 4.145 26.623 1.00 37.21 . 1 1251 ATOM O O GLU A 202 . 13.721 5.281 26.766 1.00 37.42 . 1 1252 ATOM C CB GLU A 202 . 14.833 3.151 28.797 1.00 36.84 . 1 1253 ATOM C CG GLU A 202 . 14.635 2.127 29.899 1.00 36.92 . 1 1254 ATOM C CD GLU A 202 . 15.576 2.341 31.071 1.00 35.97 . 1 1255 ATOM O OE1 GLU A 202 . 16.792 2.515 30.839 1.00 35.75 . 1 1256 ATOM O OE2 GLU A 202 . 15.094 2.330 32.226 1.00 36.16 . 1 1257 ATOM N N ILE A 203 . 14.935 3.794 25.590 1.00 36.63 . 1 1258 ATOM C CA ILE A 203 . 15.360 4.781 24.601 1.00 36.84 . 1 1259 ATOM C C ILE A 203 . 14.772 4.710 23.192 1.00 37.34 . 1 1260 ATOM O O ILE A 203 . 14.737 5.723 22.490 1.00 37.77 . 1 1261 ATOM C CB ILE A 203 . 16.894 4.764 24.453 1.00 36.41 . 1 1262 ATOM C CG1 ILE A 203 . 17.332 3.444 23.809 1.00 36.26 . 1 1263 ATOM C CG2 ILE A 203 . 17.549 4.927 25.820 1.00 36.24 . 1 1264 ATOM C CD1 ILE A 203 . 18.821 3.334 23.571 1.00 35.72 . 1 1265 ATOM N N TYR A 204 . 14.326 3.534 22.762 1.00 37.19 . 1 1266 ATOM C CA TYR A 204 . 13.776 3.395 21.418 1.00 37.90 . 1 1267 ATOM C C TYR A 204 . 12.292 3.737 21.369 1.00 38.47 . 1 1268 ATOM O O TYR A 204 . 11.498 3.237 22.160 1.00 38.39 . 1 1269 ATOM C CB TYR A 204 . 14.009 1.975 20.907 1.00 37.58 . 1 1270 ATOM C CG TYR A 204 . 13.486 1.714 19.513 1.00 36.82 . 1 1271 ATOM C CD1 TYR A 204 . 13.950 2.443 18.415 1.00 36.24 . 1 1272 ATOM C CD2 TYR A 204 . 12.554 0.704 19.285 1.00 36.68 . 1 1273 ATOM C CE1 TYR A 204 . 13.498 2.159 17.119 1.00 35.49 . 1 1274 ATOM C CE2 TYR A 204 . 12.098 0.416 18.008 1.00 36.44 . 1 1275 ATOM C CZ TYR A 204 . 12.571 1.139 16.931 1.00 36.00 . 1 1276 ATOM O OH TYR A 204 . 12.113 0.812 15.678 1.00 35.74 . 1 1277 ATOM N N THR A 205 . 11.923 4.592 20.423 1.00 39.25 . 1 1278 ATOM C CA THR A 205 . 10.538 5.025 20.282 1.00 40.05 . 1 1279 ATOM C C THR A 205 . 9.867 4.463 19.035 1.00 40.28 . 1 1280 ATOM O O THR A 205 . 8.701 4.753 18.773 1.00 41.27 . 1 1281 ATOM C CB THR A 205 . 10.468 6.556 20.211 1.00 40.32 . 1 1282 ATOM O OG1 THR A 205 . 11.258 7.013 19.104 1.00 40.18 . 1 1283 ATOM C CG2 THR A 205 . 11.013 7.166 21.488 1.00 40.61 . 1 1284 ATOM N N GLY A 206 . 10.601 3.656 18.276 1.00 40.26 . 1 1285 ATOM C CA GLY A 206 . 10.060 3.091 17.053 1.00 39.75 . 1 1286 ATOM C C GLY A 206 . 8.956 2.059 17.190 1.00 40.12 . 1 1287 ATOM O O GLY A 206 . 8.472 1.545 16.175 1.00 39.45 . 1 1288 ATOM N N PHE A 207 . 8.551 1.749 18.421 1.00 40.55 . 1 1289 ATOM C CA PHE A 207 . 7.491 0.766 18.653 1.00 41.04 . 1 1290 ATOM C C PHE A 207 . 6.072 1.333 18.592 1.00 42.48 . 1 1291 ATOM O O PHE A 207 . 5.152 0.652 18.137 1.00 42.05 . 1 1292 ATOM C CB PHE A 207 . 7.708 0.063 19.996 1.00 39.87 . 1 1293 ATOM C CG PHE A 207 . 8.810 −0.959 19.974 1.00 38.59 . 1 1294 ATOM C CD1 PHE A 207 . 9.731 −1.028 21.013 1.00 37.65 . 1 1295 ATOM C CD2 PHE A 207 . 8.922 −1.861 18.915 1.00 37.72 . 1 1296 ATOM C CE1 PHE A 207 . 10.748 −1.973 20.998 1.00 37.10 . 1 1297 ATOM C CE2 PHE A 207 . 9.933 −2.810 18.891 1.00 36.72 . 1 1298 ATOM C CZ PHE A 207 . 10.850 −2.866 19.935 1.00 37.11 . 1 1299 ATOM N N GLU A 208 . 5.884 2.563 19.066 1.00 44.19 . 1 1300 ATOM C CA GLU A 208 . 4.559 3.186 19.028 1.00 45.81 . 1 1301 ATOM C C GLU A 208 . 4.065 3.192 17.582 1.00 45.72 . 1 1302 ATOM O O GLU A 208 . 4.835 3.447 16.661 1.00 45.82 . 1 1303 ATOM C CB GLU A 208 . 4.623 4.630 19.547 1.00 47.62 . 1 1304 ATOM C CG GLU A 208 . 4.665 4.776 21.071 1.00 50.22 . 1 1305 ATOM C CD GLU A 208 . 3.304 4.572 21.722 1.00 51.78 . 1 1306 ATOM O OE1 GLU A 208 . 2.343 5.259 21.318 1.00 53.54 . 1 1307 ATOM O OE2 GLU A 208 . 3.188 3.735 22.644 1.00 52.44 . 1 1308 ATOM N N GLY A 209 . 2.787 2.894 17.381 1.00 45.87 . 1 1309 ATOM C CA GLY A 209 . 2.244 2.897 16.033 1.00 45.86 . 1 1310 ATOM C C GLY A 209 . 2.257 1.582 15.269 1.00 45.81 . 1 1311 ATOM O O GLY A 209 . 1.794 1.526 14.123 1.00 46.16 . 1 1312 ATOM N N ILE A 210 . 2.783 0.521 15.875 1.00 45.20 . 1 1313 ATOM C CA ILE A 210 . 2.819 −0.774 15.204 1.00 44.39 . 1 1314 ATOM C C ILE A 210 . 1.600 −1.623 15.563 1.00 44.38 . 1 1315 ATOM O O ILE A 210 . 1.174 −1.674 16.719 1.00 44.36 . 1 1316 ATOM C CB ILE A 210 . 4.103 −1.556 15.557 1.00 44.44 . 1 1317 ATOM C CG1 ILE A 210 . 5.329 −0.758 15.106 1.00 43.95 . 1 1318 ATOM C CG2 ILE A 210 . 4.092 −2.925 14.873 1.00 43.07 . 1 1319 ATOM C CD1 ILE A 210 . 6.651 −1.342 15.568 1.00 44.10 . 1 1320 ATOM N N SER A 211 . 1.046 −2.290 14.556 1.00 43.93 . 1 1321 ATOM C CA SER A 211 . −0.123 −3.139 14.726 1.00 43.41 . 1 1322 ATOM C C SER A 211 . 0.257 −4.578 15.061 1.00 43.20 . 1 1323 ATOM O O SER A 211 . −0.248 −5.160 16.022 1.00 43.04 . 1 1324 ATOM C CB SER A 211 . −0.963 −3.130 13.443 1.00 44.25 . 1 1325 ATOM O OG SER A 211 . −1.830 −4.254 13.405 1.00 44.54 . 1 1326 ATOM N N THR A 212 . 1.138 −5.147 14.246 1.00 42.65 . 1 1327 ATOM C CA THR A 212 . 1.586 −6.516 14.440 1.00 42.61 . 1 1328 ATOM C C THR A 212 . 3.096 −6.608 14.297 1.00 41.28 . 1 1329 ATOM O O THR A 212 . 3.653 −6.301 13.242 1.00 42.16 . 1 1330 ATOM C CB THR A 212 . 0.926 −7.464 13.423 1.00 43.65 . 1 1331 ATOM O OG1 THR A 212 . 1.704 −8.662 13.313 1.00 45.93 . 1 1332 ATOM C CG2 THR A 212 . 0.823 −6.798 12.064 1.00 44.44 . 1 1333 ATOM N N LEU A 213 . 3.757 −7.024 15.370 1.00 39.06 . 1 1334 ATOM C CA LEU A 213 . 5.206 −7.154 15.370 1.00 36.93 . 1 1335 ATOM C C LEU A 213 . 5.612 −8.622 15.251 1.00 35.68 . 1 1336 ATOM O O LEU A 213 . 5.147 −9.467 16.010 1.00 35.24 . 1 1337 ATOM C CB LEU A 213 . 5.775 −6.561 16.661 1.00 35.99 . 1 1338 ATOM C CG LEU A 213 . 7.293 −6.606 16.811 1.00 35.91 . 1 1339 ATOM C CD1 LEU A 213 . 7.926 −5.689 15.779 1.00 36.28 . 1 1340 ATOM C CD2 LEU A 213 . 7.683 −6.193 18.219 1.00 35.41 . 1 1341 ATOM N N VAL A 214 . 6.475 −8.920 14.291 1.00 34.67 . 1 1342 ATOM C CA VAL A 214 . 6.933 −10.286 14.094 1.00 34.21 . 1 1343 ATOM C C VAL A 214 . 8.384 −10.407 14.561 1.00 33.39 . 1 1344 ATOM O O VAL A 214 . 9.266 −9.726 14.044 1.00 32.51 . 1 1345 ATOM C CB VAL A 214 . 6.855 −10.702 12.597 1.00 34.10 . 1 1346 ATOM C CG1 VAL A 214 . 7.342 −12.130 12.431 1.00 34.24 . 1 1347 ATOM C CG2 VAL A 214 . 5.422 −10.568 12.086 1.00 34.55 . 1 1348 ATOM N N ASP A 215 . 8.620 −11.262 15.550 1.00 32.73 . 1 1349 ATOM C CA ASP A 215 . 9.971 −11.466 16.052 1.00 32.84 . 1 1350 ATOM C C ASP A 215 . 10.561 −12.660 15.320 1.00 31.60 . 1 1351 ATOM O O ASP A 215 . 10.282 −13.815 15.668 1.00 30.94 . 1 1352 ATOM C CB ASP A 215 . 9.961 −11.749 17.556 1.00 34.63 . 1 1353 ATOM C CG ASP A 215 . 11.320 −11.546 18.183 1.00 37.42 . 1 1354 ATOM O OD1 ASP A 215 . 12.334 −11.754 17.477 1.00 38.50 . 1 1355 ATOM O OD2 ASP A 215 . 11.382 −11.185 19.382 1.00 39.50 . 1 1356 ATOM N N VAL A 216 . 11.368 −12.364 14.306 1.00 30.70 . 1 1357 ATOM C CA VAL A 216 . 12.007 −13.371 13.466 1.00 30.33 . 1 1358 ATOM C C VAL A 216 . 13.209 −13.993 14.157 1.00 30.64 . 1 1359 ATOM O O VAL A 216 . 14.219 −13.325 14.377 1.00 30.64 . 1 1360 ATOM C CB VAL A 216 . 12.463 −12.742 12.149 1.00 29.56 . 1 1361 ATOM C CG1 VAL A 216 . 13.066 −13.802 11.246 1.00 29.11 . 1 1362 ATOM C CG2 VAL A 216 . 11.274 −12.039 11.485 1.00 29.16 . 1 1363 ATOM N N GLY A 217 . 13.102 −15.280 14.479 1.00 30.55 . 1 1364 ATOM C CA GLY A 217 . 14.180 −15.951 15.185 1.00 30.21 . 1 1365 ATOM C C GLY A 217 . 14.073 −15.528 16.643 1.00 30.57 . 1 1366 ATOM O O GLY A 217 . 15.082 −15.345 17.331 1.00 31.33 . 1 1367 ATOM N N GLY A 218 . 12.835 −15.387 17.114 1.00 30.43 . 1 1368 ATOM C CA GLY A 218 . 12.583 −14.954 18.479 1.00 30.89 . 1 1369 ATOM C C GLY A 218 . 12.713 −15.962 19.609 1.00 30.89 . 1 1370 ATOM O O GLY A 218 . 12.319 −15.677 20.738 1.00 31.06 . 1 1371 ATOM N N GLY A 219 . 13.250 −17.139 19.323 1.00 30.59 . 1 1372 ATOM C CA GLY A 219 . 13.419 −18.136 20.369 1.00 30.64 . 1 1373 ATOM C C GLY A 219 . 12.177 −18.455 21.187 1.00 30.70 . 1 1374 ATOM O O GLY A 219 . 11.148 −18.862 20.643 1.00 31.11 . 1 1375 ATOM N N SER A 220 . 12.276 −18.262 22.500 1.00 30.25 . 1 1376 ATOM C CA SER A 220 . 11.185 −18.536 23.426 1.00 30.75 . 1 1377 ATOM C C SER A 220 . 10.080 −17.485 23.416 1.00 30.62 . 1 1378 ATOM O O SER A 220 . 9.019 −17.701 23.994 1.00 30.66 . 1 1379 ATOM C CB SER A 220 . 11.733 −18.641 24.852 1.00 32.14 . 1 1380 ATOM O OG SER A 220 . 12.264 −17.389 25.271 1.00 33.63 . 1 1381 ATOM N N GLY A 221 . 10.338 −16.345 22.782 1.00 30.66 . 1 1382 ATOM C CA GLY A 221 . 9.349 −15.284 22.735 1.00 30.73 . 1 1383 ATOM C C GLY A 221 . 9.435 −14.331 23.918 1.00 31.50 . 1 1384 ATOM O O GLY A 221 . 8.605 −13.423 24.059 1.00 29.88 . 1 1385 ATOM N N ARG A 222 . 10.447 −14.505 24.763 1.00 31.78 . 1 1386 ATOM C CA ARG A 222 . 10.562 −13.653 25.942 1.00 33.63 . 1 1387 ATOM C C ARG A 222 . 10.894 −12.195 25.654 1.00 33.30 . 1 1388 ATOM O O ARG A 222 . 10.419 −11.300 26.355 1.00 32.57 . 1 1389 ATOM C CB ARG A 222 . 11.545 −14.266 26.946 1.00 35.37 . 1 1390 ATOM C CG ARG A 222 . 10.830 −14.806 28.195 1.00 39.10 . 1 1391 ATOM C CD ARG A 222 . 9.526 −15.538 27.825 1.00 41.51 . 1 1392 ATOM N NE ARG A 222 . 8.618 −15.733 28.959 1.00 43.44 . 1 1393 ATOM C CZ ARG A 222 . 8.627 −16.792 29.762 1.00 44.22 . 1 1394 ATOM N NH1 ARG A 222 . 9.496 −17.776 29.562 1.00 45.14 . 1 1395 ATOM N NH2 ARG A 222 . 7.761 −16.872 30.767 1.00 45.13 . 1 1396 ATOM N N ASN A 223 . 11.686 −11.946 24.618 1.00 33.79 . 1 1397 ATOM C CA ASN A 223 . 12.010 −10.572 24.270 1.00 34.06 . 1 1398 ATOM C C ASN A 223 . 10.744 −9.887 23.785 1.00 33.53 . 1 1399 ATOM O O ASN A 223 . 10.469 −8.749 24.165 1.00 33.01 . 1 1400 ATOM C CB ASN A 223 . 13.104 −10.526 23.207 1.00 35.52 . 1 1401 ATOM C CG ASN A 223 . 14.455 −10.923 23.760 1.00 37.29 . 1 1402 ATOM O OD1 ASN A 223 . 14.719 −10.755 24.957 1.00 39.09 . 1 1403 ATOM N ND2 ASN A 223 . 15.326 −11.434 22.899 1.00 38.04 . 1 1404 ATOM N N LEU A 224 . 9.961 −10.588 22.967 1.00 32.77 . 1 1405 ATOM C CA LEU A 224 . 8.702 −10.040 22.467 1.00 32.75 . 1 1406 ATOM C C LEU A 224 . 7.795 −9.710 23.644 1.00 32.78 . 1 1407 ATOM O O LEU A 224 . 7.159 −8.654 23.672 1.00 31.88 . 1 1408 ATOM C CB LEU A 224 . 7.974 −11.047 21.569 1.00 32.67 . 1 1409 ATOM C CG LEU A 224 . 7.603 −10.623 20.143 1.00 33.38 . 1 1410 ATOM C CD1 LEU A 224 . 6.520 −11.563 19.627 1.00 33.04 . 1 1411 ATOM C CD2 LEU A 224 . 7.114 −9.183 20.093 1.00 32.83 . 1 1412 ATOM N N GLU A 225 . 7.732 −10.619 24.616 1.00 33.07 . 1 1413 ATOM C CA GLU A 225 . 6.894 −10.414 25.793 1.00 34.13 . 1 1414 ATOM C C GLU A 225 . 7.188 −9.075 26.462 1.00 34.07 . 1 1415 ATOM O O GLU A 225 . 6.275 −8.358 26.869 1.00 33.65 . 1 1416 ATOM C CB GLU A 225 . 7.100 −11.544 26.811 1.00 35.51 . 1 1417 ATOM C CG GLU A 225 . 6.384 −11.310 28.135 1.00 37.58 . 1 1418 ATOM C CD GLU A 225 . 6.548 −12.462 29.117 1.00 40.01 . 1 1419 ATOM O OE1 GLU A 225 . 7.697 −12.896 29.354 1.00 41.39 . 1 1420 ATOM O OE2 GLU A 225 . 5.523 −12.928 29.659 1.00 41.05 . 1 1421 ATOM N N LEU A 226 . 8.469 −8.751 26.586 1.00 34.60 . 1 1422 ATOM C CA LEU A 226 . 8.880 −7.498 27.203 1.00 35.18 . 1 1423 ATOM C C LEU A 226 . 8.366 −6.289 26.427 1.00 35.02 . 1 1424 ATOM O O LEU A 226 . 7.918 −5.312 27.026 1.00 35.01 . 1 1425 ATOM C CB LEU A 226 . 10.402 −7.449 27.307 1.00 35.34 . 1 1426 ATOM C CG LEU A 226 . 10.974 −8.400 28.360 1.00 36.24 . 1 1427 ATOM C CD1 LEU A 226 . 12.482 −8.401 28.277 1.00 36.28 . 1 1428 ATOM C CD2 LEU A 226 . 10.504 −7.985 29.750 1.00 36.11 . 1 1429 ATOM N N ILE A 227 . 8.419 −6.374 25.100 1.00 34.54 . 1 1430 ATOM C CA ILE A 227 . 7.973 −5.299 24.216 1.00 34.97 . 1 1431 ATOM C C ILE A 227 . 6.464 −5.113 24.263 1.00 36.12 . 1 1432 ATOM O O ILE A 227 . 5.969 −3.985 24.344 1.00 35.85 . 1 1433 ATOM C CB ILE A 227 . 8.391 −5.581 22.753 1.00 34.59 . 1 1434 ATOM C CG1 ILE A 227 . 9.913 −5.573 22.640 1.00 33.22 . 1 1435 ATOM C CG2 ILE A 227 . 7.775 −4.546 21.814 1.00 35.04 . 1 1436 ATOM C CD1 ILE A 227 . 10.426 −5.971 21.270 1.00 33.94 . 1 1437 ATOM N N ILE A 228 . 5.736 −6.226 24.199 1.00 36.69 . 1 1438 ATOM C CA ILE A 228 . 4.283 −6.200 24.243 1.00 38.26 . 1 1439 ATOM C C ILE A 228 . 3.863 −5.725 25.622 1.00 39.32 . 1 1440 ATOM O O ILE A 228 . 2.766 −5.210 25.810 1.00 39.50 . 1 1441 ATOM C CB ILE A 228 . 3.704 −7.600 23.935 1.00 38.03 . 1 1442 ATOM C CG1 ILE A 228 . 3.904 −7.899 22.446 1.00 38.22 . 1 1443 ATOM C CG2 ILE A 228 . 2.239 −7.665 24.300 1.00 38.66 . 1 1444 ATOM C CD1 ILE A 228 . 3.395 −9.247 22.014 1.00 40.05 . 1 1445 ATOM N N SER A 229 . 4.755 −5.915 26.585 1.00 41.18 . 1 1446 ATOM C CA SER A 229 . 4.528 −5.455 27.942 1.00 43.20 . 1 1447 ATOM C C SER A 229 . 5.163 −4.071 27.995 1.00 44.29 . 1 1448 ATOM O O SER A 229 . 6.298 −3.911 28.441 1.00 44.53 . 1 1449 ATOM C CB SER A 229 . 5.217 −6.367 28.950 1.00 43.33 . 1 1450 ATOM O OG SER A 229 . 5.302 −5.723 30.210 1.00 44.81 . 1 1451 ATOM N N LYS A 230 . 4.421 −3.088 27.505 1.00 45.37 . 1 1452 ATOM C CA LYS A 230 . 4.835 −1.688 27.450 1.00 46.24 . 1 1453 ATOM C C LYS A 230 . 4.050 −1.153 26.278 1.00 46.62 . 1 1454 ATOM O O LYS A 230 . 3.705 0.028 26.223 1.00 47.23 . 1 1455 ATOM C CB LYS A 230 . 6.332 −1.533 27.173 1.00 46.00 . 1 1456 ATOM C CG LYS A 230 . 6.808 −0.086 27.237 1.00 46.08 . 1 1457 ATOM C CD LYS A 230 . 8.298 0.024 26.966 1.00 45.99 . 1 1458 ATOM C CE LYS A 230 . 8.783 1.460 27.094 1.00 45.85 . 1 1459 ATOM N NZ LYS A 230 . 8.017 2.375 26.212 1.00 46.16 . 1 1460 ATOM N N TYR A 231 . 3.773 −2.053 25.341 1.00 46.72 . 1 1461 ATOM C CA TYR A 231 . 2.993 −1.737 24.155 1.00 46.73 . 1 1462 ATOM C C TYR A 231 . 1.951 −2.839 23.974 1.00 46.64 . 1 1463 ATOM O O TYR A 231 . 1.969 −3.574 22.987 1.00 46.55 . 1 1464 ATOM C CB TYR A 231 . 3.893 −1.651 22.922 1.00 46.54 . 1 1465 ATOM C CG TYR A 231 . 4.944 −0.575 23.022 1.00 46.34 . 1 1466 ATOM C CD1 TYR A 231 . 6.260 −0.883 23.371 1.00 45.83 . 1 1467 ATOM C CD2 TYR A 231 . 4.618 0.760 22.785 1.00 46.51 . 1 1468 ATOM C CE1 TYR A 231 . 7.228 0.116 23.479 1.00 46.34 . 1 1469 ATOM C CE2 TYR A 231 . 5.575 1.767 22.892 1.00 46.09 . 1 1470 ATOM C CZ TYR A 231 . 6.874 1.443 23.237 1.00 46.01 . 1 1471 ATOM O OH TYR A 231 . 7.818 2.442 23.330 1.00 46.25 . 1 1472 ATOM N N PRO A 232 . 1.024 −2.961 24.937 1.00 46.76 . 1 1473 ATOM C CA PRO A 232 . −0.042 −3.966 24.917 1.00 46.90 . 1 1474 ATOM C C PRO A 232 . −0.970 −3.909 23.709 1.00 46.83 . 1 1475 ATOM O O PRO A 232 . −1.780 −4.809 23.505 1.00 47.69 . 1 1476 ATOM C CB PRO A 232 . −0.778 −3.716 26.232 1.00 46.84 . 1 1477 ATOM C CG PRO A 232 . −0.575 −2.255 26.459 1.00 46.83 . 1 1478 ATOM C CD PRO A 232 . 0.881 −2.079 26.108 1.00 46.78 . 1 1479 ATOM N N LEU A 233 . −0.856 −2.864 22.901 1.00 46.61 . 1 1480 ATOM C CA LEU A 233 . −1.706 −2.756 21.725 1.00 45.92 . 1 1481 ATOM C C LEU A 233 . −1.101 −3.465 20.518 1.00 45.14 . 1 1482 ATOM O O LEU A 233 . −1.756 −3.620 19.484 1.00 44.86 . 1 1483 ATOM C CB LEU A 233 . −1.971 −1.288 21.390 1.00 47.38 . 1 1484 ATOM C CG LEU A 233 . −2.873 −0.541 22.376 1.00 48.19 . 1 1485 ATOM C CD1 LEU A 233 . −3.107 0.878 21.873 1.00 48.75 . 1 1486 ATOM C CD2 LEU A 233 . −4.202 −1.284 22.520 1.00 48.83 . 1 1487 ATOM N N ILE A 234 . 0.149 −3.901 20.651 1.00 43.47 . 1 1488 ATOM C CA ILE A 234 . 0.822 −4.602 19.563 1.00 41.66 . 1 1489 ATOM C C ILE A 234 . 0.528 −6.098 19.597 1.00 40.95 . 1 1490 ATOM O O ILE A 234 . 0.675 −6.738 20.637 1.00 40.08 . 1 1491 ATOM C CB ILE A 234 . 2.358 −4.436 19.639 1.00 41.49 . 1 1492 ATOM C CG1 ILE A 234 . 2.734 −2.957 19.598 1.00 41.11 . 1 1493 ATOM C CG2 ILE A 234 . 3.016 −5.180 18.485 1.00 40.55 . 1 1494 ATOM C CD1 ILE A 234 . 4.234 −2.708 19.621 1.00 41.16 . 1 1495 ATOM N N LYS A 235 . 0.103 −6.651 18.465 1.00 40.02 . 1 1496 ATOM C CA LYS A 235 . −0.150 −8.081 18.383 1.00 39.35 . 1 1497 ATOM C C LYS A 235 . 1.181 −8.698 17.970 1.00 38.17 . 1 1498 ATOM O O LYS A 235 . 1.742 −8.351 16.930 1.00 38.31 . 1 1499 ATOM C CB LYS A 235 . −1.247 −8.393 17.359 1.00 40.54 . 1 1500 ATOM C CG LYS A 235 . −2.646 −8.066 17.878 1.00 41.69 . 1 1501 ATOM C CD LYS A 235 . −3.722 −8.929 17.242 1.00 43.83 . 1 1502 ATOM C CE LYS A 235 . −5.068 −8.712 17.936 1.00 44.63 . 1 1503 ATOM N NZ LYS A 235 . −6.119 −9.687 17.504 1.00 46.04 . 1 1504 ATOM N N GLY A 236 . 1.692 −9.600 18.799 1.00 35.94 . 1 1505 ATOM C CA GLY A 236 . 2.978 −10.196 18.509 1.00 33.97 . 1 1506 ATOM C C GLY A 236 . 2.994 −11.607 17.969 1.00 32.51 . 1 1507 ATOM O O GLY A 236 . 2.175 −12.447 18.328 1.00 32.06 . 1 1508 ATOM N N ILE A 237 . 3.945 −11.857 17.081 1.00 31.38 . 1 1509 ATOM C CA ILE A 237 . 4.122 −13.179 16.509 1.00 31.44 . 1 1510 ATOM C C ILE A 237 . 5.567 −13.581 16.750 1.00 30.12 . 1 1511 ATOM O O ILE A 237 . 6.493 −12.933 16.262 1.00 29.73 . 1 1512 ATOM C CB ILE A 237 . 3.830 −13.208 14.979 1.00 31.46 . 1 1513 ATOM C CG1 ILE A 237 . 2.327 −13.054 14.727 1.00 32.43 . 1 1514 ATOM C CG2 ILE A 237 . 4.324 −14.520 14.382 1.00 32.12 . 1 1515 ATOM C CD1 ILE A 237 . 1.961 −12.936 13.248 1.00 32.26 . 1 1516 ATOM N N ASN A 238 . 5.758 −14.636 17.531 1.00 28.98 . 1 1517 ATOM C CA ASN A 238 . 7.099 −15.121 17.797 1.00 28.30 . 1 1518 ATOM C C ASN A 238 . 7.337 −16.231 16.790 1.00 27.69 . 1 1519 ATOM O O ASN A 238 . 6.666 −17.257 16.828 1.00 27.20 . 1 1520 ATOM C CB ASN A 238 . 7.217 −15.654 19.225 1.00 28.68 . 1 1521 ATOM C CG ASN A 238 . 8.570 −16.258 19.492 1.00 29.83 . 1 1522 ATOM O OD1 ASN A 238 . 9.593 −15.690 19.110 1.00 30.85 . 1 1523 ATOM N ND2 ASN A 238 . 8.591 −17.411 20.143 1.00 30.35 . 1 1524 ATOM N N PHE A 239 . 8.300 −16.016 15.901 1.00 27.76 . 1 1525 ATOM C CA PHE A 239 . 8.607 −16.950 14.817 1.00 28.66 . 1 1526 ATOM C C PHE A 239 . 9.985 −17.578 14.925 1.00 29.44 . 1 1527 ATOM O O PHE A 239 . 10.993 −16.878 14.983 1.00 30.42 . 1 1528 ATOM C CB PHE A 239 . 8.482 −16.203 13.477 1.00 27.96 . 1 1529 ATOM C CG PHE A 239 . 8.786 −17.042 12.265 1.00 28.14 . 1 1530 ATOM C CD1 PHE A 239 . 7.918 −18.054 11.863 1.00 28.22 . 1 1531 ATOM C CD2 PHE A 239 . 9.931 −16.806 11.515 1.00 28.00 . 1 1532 ATOM C CE1 PHE A 239 . 8.187 −18.820 10.724 1.00 28.36 . 1 1533 ATOM C CE2 PHE A 239 . 10.212 −17.562 10.379 1.00 29.31 . 1 1534 ATOM C CZ PHE A 239 . 9.333 −18.574 9.981 1.00 28.61 . 1 1535 ATOM N N ASP A 240 . 10.029 −18.905 14.941 1.00 29.53 . 1 1536 ATOM C CA ASP A 240 . 11.294 −19.617 15.028 1.00 30.48 . 1 1537 ATOM C C ASP A 240 . 11.105 −21.030 14.465 1.00 31.49 . 1 1538 ATOM O O ASP A 240 . 10.012 −21.390 14.016 1.00 32.03 . 1 1539 ATOM C CB ASP A 240 . 11.761 −19.675 16.493 1.00 29.68 . 1 1540 ATOM C CG ASP A 240 . 13.274 −19.714 16.626 1.00 30.48 . 1 1541 ATOM O OD1 ASP A 240 . 13.885 −20.737 16.242 1.00 30.08 . 1 1542 ATOM O OD2 ASP A 240 . 13.862 −18.714 17.108 1.00 29.89 . 1 1543 ATOM N N LEU A 241 . 12.174 −21.818 14.485 1.00 32.31 . 1 1544 ATOM C CA LEU A 241 . 12.142 −23.195 13.989 1.00 33.37 . 1 1545 ATOM C C LEU A 241 . 11.106 −24.017 14.740 1.00 33.87 . 1 1546 ATOM O O LEU A 241 . 10.913 −23.843 15.948 1.00 33.29 . 1 1547 ATOM C CB LEU A 241 . 13.511 −23.845 14.163 1.00 33.60 . 1 1548 ATOM C CG LEU A 241 . 14.637 −23.204 13.364 1.00 34.07 . 1 1549 ATOM C CD1 LEU A 241 . 15.978 −23.734 13.854 1.00 34.09 . 1 1550 ATOM C CD2 LEU A 241 . 14.429 −23.493 11.882 1.00 34.49 . 1 1551 ATOM N N PRO A 242 . 10.421 −24.930 14.036 1.00 34.44 . 1 1552 ATOM C CA PRO A 242 . 9.414 −25.742 14.718 1.00 34.78 . 1 1553 ATOM C C PRO A 242 . 9.927 −26.438 15.983 1.00 35.08 . 1 1554 ATOM O O PRO A 242 . 9.211 −26.513 16.984 1.00 35.19 . 1 1555 ATOM C CB PRO A 242 . 8.949 −26.719 13.626 1.00 34.94 . 1 1556 ATOM C CG PRO A 242 . 10.087 −26.747 12.644 1.00 35.17 . 1 1557 ATOM C CD PRO A 242 . 10.545 −25.311 12.618 1.00 34.52 . 1 1558 ATOM N N GLN A 243 . 11.164 −26.926 15.947 1.00 35.65 . 1 1559 ATOM C CA GLN A 243 . 11.730 −27.609 17.107 1.00 36.36 . 1 1560 ATOM C C GLN A 243 . 11.913 −26.662 18.282 1.00 36.88 . 1 1561 ATOM O O GLN A 243 . 11.968 −27.092 19.437 1.00 36.99 . 1 1562 ATOM C CB GLN A 243 . 13.072 −28.262 16.761 1.00 37.51 . 1 1563 ATOM C CG GLN A 243 . 14.100 −27.344 16.112 1.00 39.23 . 1 1564 ATOM C CD GLN A 243 . 14.148 −27.487 14.598 1.00 39.40 . 1 1565 ATOM O OE1 GLN A 243 . 13.130 −27.375 13.919 1.00 39.66 . 1 1566 ATOM N NE2 GLN A 243 . 15.342 −27.729 14.064 1.00 40.54 . 1 1567 ATOM N N VAL A 244 . 12.007 −25.369 17.984 1.00 36.16 . 1 1568 ATOM C CA VAL A 244 . 12.167 −24.365 19.027 1.00 35.63 . 1 1569 ATOM C C VAL A 244 . 10.792 −23.955 19.556 1.00 35.67 . 1 1570 ATOM O O VAL A 244 . 10.574 −23.899 20.772 1.00 33.84 . 1 1571 ATOM C CB VAL A 244 . 12.909 −23.119 18.490 1.00 34.90 . 1 1572 ATOM C CG1 VAL A 244 . 12.922 −22.028 19.541 1.00 35.30 . 1 1573 ATOM C CG2 VAL A 244 . 14.330 −23.493 18.105 1.00 33.70 . 1 1574 ATOM N N ILE A 245 . 9.866 −23.684 18.639 1.00 35.83 . 1 1575 ATOM C CA ILE A 245 . 8.517 −23.281 19.013 1.00 36.81 . 1 1576 ATOM C C ILE A 245 . 7.837 −24.304 19.927 1.00 38.57 . 1 1577 ATOM O O ILE A 245 . 7.072 −23.927 20.817 1.00 37.98 . 1 1578 ATOM C CB ILE A 245 . 7.647 −23.027 17.752 1.00 37.02 . 1 1579 ATOM C CG1 ILE A 245 . 8.196 −21.824 16.979 1.00 36.73 . 1 1580 ATOM C CG2 ILE A 245 . 6.203 −22.753 18.140 1.00 37.12 . 1 1581 ATOM C CD1 ILE A 245 . 8.210 −20.528 17.773 1.00 36.65 . 1 1582 ATOM N N GLU A 246 . 8.108 −25.593 19.723 1.00 40.37 . 1 1583 ATOM C CA GLU A 246 . 7.504 −26.613 20.580 1.00 42.50 . 1 1584 ATOM C C GLU A 246 . 8.342 −26.825 21.842 1.00 42.76 . 1 1585 ATOM O O GLU A 246 . 8.976 −27.866 22.029 1.00 44.31 . 1 1586 ATOM C CB GLU A 246 . 7.333 −27.941 19.831 1.00 44.03 . 1 1587 ATOM C CG GLU A 246 . 8.612 −28.703 19.536 1.00 46.78 . 1 1588 ATOM C CD GLU A 246 . 8.334 −30.095 18.987 1.00 49.04 . 1 1589 ATOM O OE1 GLU A 246 . 7.890 −30.204 17.823 1.00 50.46 . 1 1590 ATOM O OE2 GLU A 246 . 8.547 −31.082 19.726 1.00 50.35 . 1 1591 ATOM N N ASN A 247 . 8.343 −25.805 22.689 1.00 42.48 . 1 1592 ATOM C CA ASN A 247 . 9.052 −25.769 23.972 1.00 41.68 . 1 1593 ATOM C C ASN A 247 . 8.893 −24.333 24.445 1.00 40.77 . 1 1594 ATOM O O ASN A 247 . 9.326 −23.962 25.533 1.00 40.42 . 1 1595 ATOM C CB ASN A 247 . 10.545 −26.103 23.829 1.00 41.86 . 1 1596 ATOM C CG ASN A 247 . 10.802 −27.594 23.720 1.00 42.41 . 1 1597 ATOM O OD1 ASN A 247 . 10.284 −28.385 24.509 1.00 42.85 . 1 1598 ATOM N ND2 ASN A 247 . 11.604 −27.985 22.741 1.00 42.84 . 1 1599 ATOM N N ALA A 248 . 8.265 −23.530 23.594 1.00 40.12 . 1 1600 ATOM C CA ALA A 248 . 8.011 −22.132 23.899 1.00 39.20 . 1 1601 ATOM C C ALA A 248 . 6.834 −22.068 24.857 1.00 38.34 . 1 1602 ATOM O O ALA A 248 . 5.809 −22.711 24.644 1.00 37.98 . 1 1603 ATOM C CB ALA A 248 . 7.692 −21.362 22.625 1.00 39.51 . 1 1604 ATOM N N PRO A 249 . 6.971 −21.292 25.936 1.00 37.94 . 1 1605 ATOM C CA PRO A 249 . 5.881 −21.180 26.901 1.00 37.61 . 1 1606 ATOM C C PRO A 249 . 4.776 −20.303 26.348 1.00 36.97 . 1 1607 ATOM O O PRO A 249 . 5.030 −19.405 25.550 1.00 37.30 . 1 1608 ATOM C CB PRO A 249 . 6.561 −20.536 28.096 1.00 37.50 . 1 1609 ATOM C CG PRO A 249 . 7.503 −19.582 27.430 1.00 37.31 . 1 1610 ATOM C CD PRO A 249 . 8.109 −20.442 26.335 1.00 38.26 . 1 1611 ATOM N N PRO A 250 . 3.528 −20.559 26.756 1.00 37.02 . 1 1612 ATOM C CA PRO A 250 . 2.420 −19.737 26.265 1.00 36.88 . 1 1613 ATOM C C PRO A 250 . 2.558 −18.334 26.863 1.00 36.85 . 1 1614 ATOM O O PRO A 250 . 2.825 −18.186 28.060 1.00 36.60 . 1 1615 ATOM C CB PRO A 250 . 1.190 −20.484 26.768 1.00 36.83 . 1 1616 ATOM C CG PRO A 250 . 1.685 −21.156 28.020 1.00 36.88 . 1 1617 ATOM C CD PRO A 250 . 3.045 −21.651 27.618 1.00 37.24 . 1 1618 ATOM N N LEU A 251 . 2.396 −17.314 26.027 1.00 36.77 . 1 1619 ATOM C CA LEU A 251 . 2.523 −15.926 26.475 1.00 36.94 . 1 1620 ATOM C C LEU A 251 . 1.335 −15.104 25.976 1.00 37.30 . 1 1621 ATOM O O LEU A 251 . 0.982 −15.163 24.798 1.00 37.62 . 1 1622 ATOM C CB LEU A 251 . 3.831 −15.338 25.935 1.00 36.25 . 1 1623 ATOM C CG LEU A 251 . 5.113 −16.136 26.204 1.00 35.80 . 1 1624 ATOM C CD1 LEU A 251 . 6.199 −15.693 25.242 1.00 36.30 . 1 1625 ATOM C CD2 LEU A 251 . 5.550 −15.959 27.645 1.00 35.49 . 1 1626 ATOM N N SER A 252 . 0.721 −14.332 26.866 1.00 37.92 . 1 1627 ATOM C CA SER A 252 . −0.436 −13.526 26.485 1.00 38.60 . 1 1628 ATOM C C SER A 252 . −0.099 −12.488 25.417 1.00 37.86 . 1 1629 ATOM O O SER A 252 . 0.920 −11.802 25.500 1.00 38.16 . 1 1630 ATOM C CB SER A 252 . −1.040 −12.830 27.716 1.00 39.96 . 1 1631 ATOM O OG SER A 252 . −0.119 −11.942 28.333 1.00 42.41 . 1 1632 ATOM N N GLY A 253 . −0.964 −12.393 24.409 1.00 36.91 . 1 1633 ATOM C CA GLY A 253 . −0.757 −11.443 23.332 1.00 35.58 . 1 1634 ATOM C C GLY A 253 . 0.265 −11.881 22.300 1.00 34.77 . 1 1635 ATOM O O GLY A 253 . 0.590 −11.123 21.380 1.00 34.71 . 1 1636 ATOM N N ILE A 254 . 0.772 −13.105 22.435 1.00 33.82 . 1 1637 ATOM C CA ILE A 254 . 1.772 −13.613 21.503 1.00 32.75 . 1 1638 ATOM C C ILE A 254 . 1.399 −14.946 20.878 1.00 33.06 . 1 1639 ATOM O O ILE A 254 . 0.985 −15.882 21.561 1.00 31.72 . 1 1640 ATOM C CB ILE A 254 . 3.158 −13.764 22.189 1.00 32.61 . 1 1641 ATOM C CG1 ILE A 254 . 3.675 −12.379 22.613 1.00 31.98 . 1 1642 ATOM C CG2 ILE A 254 . 4.143 −14.445 21.240 1.00 31.17 . 1 1643 ATOM C CD1 ILE A 254 . 4.916 −12.401 23.471 1.00 31.75 . 1 1644 ATOM N N GLU A 255 . 1.574 −15.016 19.568 1.00 33.55 . 1 1645 ATOM C CA GLU A 255 . 1.274 −16.210 18.801 1.00 34.32 . 1 1646 ATOM C C GLU A 255 . 2.583 −16.849 18.367 1.00 33.31 . 1 1647 ATOM O O GLU A 255 . 3.381 −16.218 17.693 1.00 33.04 . 1 1648 ATOM C CB GLU A 255 . 0.455 −15.830 17.559 1.00 37.12 . 1 1649 ATOM C CG GLU A 255 . −0.097 −17.004 16.764 1.00 39.89 . 1 1650 ATOM C CD GLU A 255 . −0.656 −16.573 15.412 1.00 42.36 . 1 1651 ATOM O OE1 GLU A 255 . −1.122 −15.412 15.302 1.00 43.27 . 1 1652 ATOM O OE2 GLU A 255 . −0.638 −17.396 14.465 1.00 43.55 . 1 1653 ATOM N N HIS A 256 . 2.806 −18.098 18.756 1.00 32.57 . 1 1654 ATOM C CA HIS A 256 . 4.021 −18.792 18.362 1.00 32.35 . 1 1655 ATOM C C HIS A 256 . 3.785 −19.449 17.009 1.00 33.01 . 1 1656 ATOM O O HIS A 256 . 2.806 −20.181 16.824 1.00 33.52 . 1 1657 ATOM C CB HIS A 256 . 4.396 −19.855 19.390 1.00 31.76 . 1 1658 ATOM C CG HIS A 256 . 4.848 −19.297 20.699 1.00 30.89 . 1 1659 ATOM N ND1 HIS A 256 . 6.002 −18.554 20.835 1.00 30.17 . 1 1660 ATOM C CD2 HIS A 256 . 4.304 −19.375 21.936 1.00 30.30 . 1 1661 ATOM C CE1 HIS A 256 . 6.150 −18.203 22.098 1.00 30.30 . 1 1662 ATOM N NE2 HIS A 256 . 5.132 −18.687 22.788 1.00 30.26 . 1 1663 ATOM N N VAL A 257 . 4.685 −19.175 16.071 1.00 32.39 . 1 1664 ATOM C CA VAL A 257 . 4.599 −19.713 14.725 1.00 32.40 . 1 1665 ATOM C C VAL A 257 . 5.897 −20.414 14.354 1.00 32.40 . 1 1666 ATOM O O VAL A 257 . 6.956 −19.792 14.341 1.00 31.96 . 1 1667 ATOM C CB VAL A 257 . 4.341 −18.585 13.696 1.00 31.49 . 1 1668 ATOM C CG1 VAL A 257 . 4.359 −19.151 12.278 1.00 30.49 . 1 1669 ATOM C CG2 VAL A 257 . 3.009 −17.908 13.998 1.00 31.06 . 1 1670 ATOM N N GLY A 258 . 5.808 −21.707 14.047 1.00 32.66 . 1 1671 ATOM C CA GLY A 258 . 6.988 −22.459 13.670 1.00 33.21 . 1 1672 ATOM C C GLY A 258 . 7.177 −22.450 12.167 1.00 34.21 . 1 1673 ATOM O O GLY A 258 . 6.203 −22.519 11.410 1.00 34.35 . 1 1674 ATOM N N GLY A 259 . 8.431 −22.370 11.731 1.00 34.38 . 1 1675 ATOM C CA GLY A 259 . 8.720 −22.346 10.310 1.00 34.84 . 1 1676 ATOM C C GLY A 259 . 10.191 −22.131 10.025 1.00 35.16 . 1 1677 ATOM O O GLY A 259 . 11.035 −22.343 10.892 1.00 35.50 . 1 1678 ATOM N N ASP A 260 . 10.497 −21.702 8.804 1.00 35.34 . 1 1679 ATOM C CA ASP A 260 . 11.869 −21.460 8.371 1.00 35.26 . 1 1680 ATOM C C ASP A 260 . 11.963 −20.105 7.664 1.00 34.67 . 1 1681 ATOM O O ASP A 260 . 11.323 −19.887 6.637 1.00 34.79 . 1 1682 ATOM C CB ASP A 260 . 12.297 −22.601 7.445 1.00 36.80 . 1 1683 ATOM C CG ASP A 260 . 13.546 −22.287 6.660 1.00 38.36 . 1 1684 ATOM O OD1 ASP A 260 . 14.479 −21.685 7.224 1.00 39.79 . 1 1685 ATOM O OD2 ASP A 260 . 13.600 −22.662 5.470 1.00 40.08 . 1 1686 HETA N N MSE A 261 . 12.767 −19.197 8.215 1.00 33.14 . 1 1687 HETA C CA MSE A 261 . 12.910 −17.855 7.651 1.00 32.26 . 1 1688 HETA C C MSE A 261 . 13.535 −17.825 6.268 1.00 33.21 . 1 1689 HETA O O MSE A 261 . 13.424 −16.820 5.561 1.00 31.87 . 1 1690 HETA C CB MSE A 261 . 13.700 −16.936 8.597 1.00 29.16 . 1 1691 HETA C CG MSE A 261 . 15.120 −17.361 8.896 1.00 26.49 . 1 1692 HETA SE SE MSE A 261 . 15.919 −16.373 10.231 1.00 19.67 . 1 1693 HETA C CE MSE A 261 . 17.486 −16.869 10.022 1.00 20.36 . 1 1694 ATOM N N PHE A 262 . 14.189 −18.917 5.882 1.00 34.48 . 1 1695 ATOM C CA PHE A 262 . 14.796 −18.984 4.561 1.00 35.71 . 1 1696 ATOM C C PHE A 262 . 13.737 −19.297 3.500 1.00 36.55 . 1 1697 ATOM O O PHE A 262 . 13.966 −19.086 2.310 1.00 36.43 . 1 1698 ATOM C CB PHE A 262 . 15.910 −20.036 4.526 1.00 35.75 . 1 1699 ATOM C CG PHE A 262 . 17.160 −19.616 5.250 1.00 34.72 . 1 1700 ATOM C CD1 PHE A 262 . 17.574 −20.285 6.398 1.00 35.09 . 1 1701 ATOM C CD2 PHE A 262 . 17.910 −18.532 4.799 1.00 34.63 . 1 1702 ATOM C CE1 PHE A 262 . 18.722 −19.877 7.095 1.00 34.86 . 1 1703 ATOM C CE2 PHE A 262 . 19.058 −18.116 5.485 1.00 35.04 . 1 1704 ATOM C CZ PHE A 262 . 19.462 −18.791 6.636 1.00 34.66 . 1 1705 ATOM N N ALA A 263 . 12.586 −19.795 3.944 1.00 37.46 . 1 1706 ATOM C CA ALA A 263 . 11.480 −20.121 3.048 1.00 38.30 . 1 1707 ATOM C C ALA A 263 . 10.530 −18.931 2.984 1.00 38.65 . 1 1708 ATOM O O ALA A 263 . 10.223 −18.430 1.904 1.00 38.71 . 1 1709 ATOM C CB ALA A 263 . 10.741 −21.349 3.550 1.00 38.28 . 1 1710 ATOM N N SER A 264 . 10.071 −18.484 4.153 1.00 38.86 . 1 1711 ATOM C CA SER A 264 . 9.168 −17.341 4.259 1.00 38.56 . 1 1712 ATOM C C SER A 264 . 8.983 −16.964 5.726 1.00 38.76 . 1 1713 ATOM O O SER A 264 . 9.237 −17.783 6.616 1.00 38.31 . 1 1714 ATOM C CB SER A 264 . 7.801 −17.673 3.656 1.00 38.95 . 1 1715 ATOM O OG SER A 264 . 7.102 −18.605 4.462 1.00 40.06 . 1 1716 ATOM N N VAL A 265 . 8.549 −15.728 5.971 1.00 38.33 . 1 1717 ATOM C CA VAL A 265 . 8.313 −15.241 7.332 1.00 38.31 . 1 1718 ATOM C C VAL A 265 . 6.880 −14.722 7.456 1.00 38.18 . 1 1719 ATOM O O VAL A 265 . 6.283 −14.277 6.473 1.00 38.18 . 1 1720 ATOM C CB VAL A 265 . 9.293 −14.097 7.718 1.00 38.15 . 1 1721 ATOM C CG1 VAL A 265 . 10.729 −14.551 7.535 1.00 38.11 . 1 1722 ATOM C CG2 VAL A 265 . 9.026 −12.873 6.879 1.00 38.95 . 1 1723 ATOM N N PRO A 266 . 6.303 −14.789 8.665 1.00 38.07 . 1 1724 ATOM C CA PRO A 266 . 4.933 −14.314 8.879 1.00 38.14 . 1 1725 ATOM C C PRO A 266 . 4.761 −12.839 8.513 1.00 38.49 . 1 1726 ATOM O O PRO A 266 . 5.680 −12.035 8.668 1.00 38.35 . 1 1727 ATOM C CB PRO A 266 . 4.709 −14.580 10.365 1.00 37.47 . 1 1728 ATOM C CG PRO A 266 . 5.540 −15.808 10.604 1.00 37.24 . 1 1729 ATOM C CD PRO A 266 . 6.814 −15.470 9.868 1.00 37.64 . 1 1730 ATOM N N GLN A 267 . 3.578 −12.487 8.027 1.00 38.84 . 1 1731 ATOM C CA GLN A 267 . 3.312 −11.113 7.643 1.00 39.24 . 1 1732 ATOM C C GLN A 267 . 3.036 −10.204 8.831 1.00 38.74 . 1 1733 ATOM O O GLN A 267 . 2.536 −10.641 9.866 1.00 38.68 . 1 1734 ATOM C CB GLN A 267 . 2.136 −11.058 6.671 1.00 40.48 . 1 1735 ATOM C CG GLN A 267 . 2.486 −11.540 5.274 1.00 42.13 . 1 1736 ATOM C CD GLN A 267 . 1.343 −11.357 4.310 1.00 43.04 . 1 1737 ATOM O OE1 GLN A 267 . 0.306 −12.004 4.437 1.00 43.67 . 1 1738 ATOM N NE2 GLN A 267 . 1.520 −10.463 3.340 1.00 43.77 . 1 1739 ATOM N N GLY A 268 . 3.365 −8.930 8.657 1.00 38.48 . 1 1740 ATOM C CA GLY A 268 . 3.154 −7.939 9.692 1.00 38.75 . 1 1741 ATOM C C GLY A 268 . 3.676 −6.623 9.166 1.00 38.50 . 1 1742 ATOM O O GLY A 268 . 4.278 −6.594 8.096 1.00 38.27 . 1 1743 ATOM N N ASP A 269 . 3.452 −5.533 9.890 1.00 39.31 . 1 1744 ATOM C CA ASP A 269 . 3.939 −4.235 9.435 1.00 39.82 . 1 1745 ATOM C C ASP A 269 . 5.299 −3.902 10.018 1.00 39.43 . 1 1746 ATOM O O ASP A 269 . 5.899 −2.868 9.698 1.00 40.12 . 1 1747 ATOM C CB ASP A 269 . 2.945 −3.124 9.782 1.00 42.06 . 1 1748 ATOM C CG ASP A 269 . 2.355 −3.268 11.169 1.00 44.25 . 1 1749 ATOM O OD1 ASP A 269 . 1.576 −4.218 11.386 1.00 46.14 . 1 1750 ATOM O OD2 ASP A 269 . 2.659 −2.423 12.040 1.00 45.85 . 1 1751 ATOM N N ALA A 270 . 5.789 −4.785 10.879 1.00 37.95 . 1 1752 ATOM C CA ALA A 270 . 7.084 −4.583 11.499 1.00 36.03 . 1 1753 ATOM C C ALA A 270 . 7.640 −5.913 11.967 1.00 34.74 . 1 1754 ATOM O O ALA A 270 . 6.910 −6.771 12.456 1.00 34.46 . 1 1755 ATOM C CB ALA A 270 . 6.962 −3.622 12.675 1.00 36.49 . 1 1756 HETA N N MSE A 271 . 8.940 −6.082 11.788 1.00 33.30 . 1 1757 HETA C CA MSE A 271 . 9.608 −7.295 12.217 1.00 32.20 . 1 1758 HETA C C MSE A 271 . 10.847 −6.889 12.981 1.00 31.49 . 1 1759 HETA O O MSE A 271 . 11.405 −5.821 12.752 1.00 31.62 . 1 1760 HETA C CB MSE A 271 . 9.972 −8.151 11.011 1.00 31.43 . 1 1761 HETA C CG MSE A 271 . 8.728 −8.645 10.278 1.00 32.48 . 1 1762 HETA SE SE MSE A 271 . 9.081 −9.301 8.669 1.00 31.97 . 1 1763 HETA C CE MSE A 271 . 7.409 −9.145 7.908 1.00 33.04 . 1 1764 ATOM N N ILE A 272 . 11.259 −7.729 13.917 1.00 30.26 . 1 1765 ATOM C CA ILE A 272 . 12.438 −7.423 14.693 1.00 29.66 . 1 1766 ATOM C C ILE A 272 . 13.349 −8.639 14.721 1.00 28.98 . 1 1767 ATOM O O ILE A 272 . 12.900 −9.759 14.945 1.00 28.42 . 1 1768 ATOM C CB ILE A 272 . 12.045 −6.964 16.127 1.00 30.28 . 1 1769 ATOM C CG1 ILE A 272 . 13.299 −6.608 16.930 1.00 30.50 . 1 1770 ATOM C CG2 ILE A 272 . 11.206 −8.022 16.810 1.00 29.99 . 1 1771 ATOM C CD1 ILE A 272 . 12.982 −5.973 18.277 1.00 32.14 . 1 1772 ATOM N N LEU A 273 . 14.620 −8.402 14.426 1.00 28.32 . 1 1773 ATOM C CA LEU A 273 . 15.638 −9.437 14.415 1.00 28.78 . 1 1774 ATOM C C LEU A 273 . 16.730 −9.060 15.409 1.00 29.13 . 1 1775 ATOM O O LEU A 273 . 17.537 −8.147 15.167 1.00 28.65 . 1 1776 ATOM C CB LEU A 273 . 16.244 −9.584 13.020 1.00 28.56 . 1 1777 ATOM C CG LEU A 273 . 15.384 −10.289 11.963 1.00 28.48 . 1 1778 ATOM C CD1 LEU A 273 . 14.153 −9.451 11.643 1.00 28.93 . 1 1779 ATOM C CD2 LEU A 273 . 16.209 −10.503 10.710 1.00 29.46 . 1 1780 ATOM N N LYS A 274 . 16.742 −9.747 16.541 1.00 29.46 . 1 1781 ATOM C CA LYS A 274 . 17.747 −9.474 17.553 1.00 29.72 . 1 1782 ATOM C C LYS A 274 . 18.738 −10.614 17.616 1.00 29.68 . 1 1783 ATOM O O LYS A 274 . 18.360 −11.771 17.836 1.00 29.49 . 1 1784 ATOM C CB LYS A 274 . 17.105 −9.293 18.924 1.00 30.56 . 1 1785 ATOM C CG LYS A 274 . 18.135 −9.008 20.009 1.00 31.44 . 1 1786 ATOM C CD LYS A 274 . 17.509 −9.017 21.393 1.00 33.01 . 1 1787 ATOM C CE LYS A 274 . 18.564 −8.717 22.464 1.00 33.85 . 1 1788 ATOM N NZ LYS A 274 . 19.819 −9.487 22.227 1.00 33.69 . 1 1789 ATOM N N ALA A 275 . 20.008 −10.287 17.415 1.00 29.30 . 1 1790 ATOM C CA ALA A 275 . 21.055 −11.287 17.464 1.00 29.82 . 1 1791 ATOM C C ALA A 275 . 20.797 −12.435 16.488 1.00 29.99 . 1 1792 ATOM O O ALA A 275 . 21.020 −13.599 16.810 1.00 30.05 . 1 1793 ATOM C CB ALA A 275 . 21.200 −11.825 18.905 1.00 29.28 . 1 1794 ATOM N N VAL A 276 . 20.330 −12.104 15.288 1.00 30.45 . 1 1795 ATOM C CA VAL A 276 . 20.085 −13.117 14.269 1.00 30.25 . 1 1796 ATOM C C VAL A 276 . 21.128 −12.969 13.157 1.00 30.65 . 1 1797 ATOM O O VAL A 276 . 21.865 −13.908 12.854 1.00 30.60 . 1 1798 ATOM C CB VAL A 276 . 18.665 −12.976 13.662 1.00 30.81 . 1 1799 ATOM C CG1 VAL A 276 . 18.514 −13.907 12.460 1.00 30.54 . 1 1800 ATOM C CG2 VAL A 276 . 17.611 −13.292 14.715 1.00 29.51 . 1 1801 ATOM N N CYS A 277 . 21.203 −11.777 12.573 1.00 31.60 . 1 1802 ATOM C CA CYS A 277 . 22.141 −11.490 11.482 1.00 32.99 . 1 1803 ATOM C C CYS A 277 . 23.608 −11.832 11.720 1.00 32.92 . 1 1804 ATOM O O CYS A 277 . 24.283 −12.320 10.809 1.00 32.49 . 1 1805 ATOM C CB CYS A 277 . 22.062 −10.010 11.082 1.00 34.13 . 1 1806 ATOM S SG CYS A 277 . 20.505 −9.496 10.329 1.00 38.64 . 1 1807 ATOM N N HIS A 278 . 24.121 −11.570 12.921 1.00 32.83 . 1 1808 ATOM C CA HIS A 278 . 25.526 −11.859 13.159 1.00 32.82 . 1 1809 ATOM C C HIS A 278 . 25.849 −13.344 13.106 1.00 32.07 . 1 1810 ATOM O O HIS A 278 . 27.010 −13.732 13.129 1.00 31.80 . 1 1811 ATOM C CB HIS A 278 . 26.023 −11.217 14.471 1.00 34.39 . 1 1812 ATOM C CG HIS A 278 . 25.483 −11.841 15.721 1.00 35.80 . 1 1813 ATOM N ND1 HIS A 278 . 24.140 −11.889 16.013 1.00 36.66 . 1 1814 ATOM C CD2 HIS A 278 . 26.116 −12.415 16.771 1.00 37.34 . 1 1815 ATOM C CE1 HIS A 278 . 23.966 −12.470 17.188 1.00 37.11 . 1 1816 ATOM N NE2 HIS A 278 . 25.150 −12.798 17.670 1.00 37.31 . 1 1817 ATOM N N ASN A 279 . 24.820 −14.174 12.991 1.00 31.45 . 1 1818 ATOM C CA ASN A 279 . 25.021 −15.616 12.902 1.00 31.70 . 1 1819 ATOM C C ASN A 279 . 25.222 −16.069 11.457 1.00 31.69 . 1 1820 ATOM O O ASN A 279 . 25.680 −17.179 11.209 1.00 31.88 . 1 1821 ATOM C CB ASN A 279 . 23.813 −16.363 13.476 1.00 32.26 . 1 1822 ATOM C CG ASN A 279 . 23.677 −16.189 14.976 1.00 32.54 . 1 1823 ATOM O OD1 ASN A 279 . 24.617 −16.439 15.716 1.00 33.08 . 1 1824 ATOM N ND2 ASN A 279 . 22.502 −15.764 15.427 1.00 32.72 . 1 1825 ATOM N N TRP A 280 . 24.907 −15.207 10.499 1.00 32.07 . 1 1826 ATOM C CA TRP A 280 . 25.018 −15.608 9.099 1.00 32.51 . 1 1827 ATOM C C TRP A 280 . 25.867 −14.742 8.196 1.00 33.13 . 1 1828 ATOM O O TRP A 280 . 26.128 −13.578 8.488 1.00 32.57 . 1 1829 ATOM C CB TRP A 280 . 23.626 −15.704 8.491 1.00 32.13 . 1 1830 ATOM C CG TRP A 280 . 22.673 −16.500 9.307 1.00 31.25 . 1 1831 ATOM C CD1 TRP A 280 . 21.902 −16.052 10.338 1.00 31.32 . 1 1832 ATOM C CD2 TRP A 280 . 22.383 −17.887 9.161 1.00 30.87 . 1 1833 ATOM N NE1 TRP A 280 . 21.144 −17.078 10.843 1.00 30.55 . 1 1834 ATOM C CE2 TRP A 280 . 21.420 −18.218 10.135 1.00 30.46 . 1 1835 ATOM C CE3 TRP A 280 . 22.841 −18.886 8.294 1.00 30.80 . 1 1836 ATOM C CZ2 TRP A 280 . 20.905 −19.509 10.270 1.00 31.19 . 1 1837 ATOM C CZ3 TRP A 280 . 22.326 −20.171 8.428 1.00 31.02 . 1 1838 ATOM C CH2 TRP A 280 . 21.370 −20.470 9.406 1.00 30.93 . 1 1839 ATOM N N SER A 281 . 26.279 −15.330 7.075 1.00 34.04 . 1 1840 ATOM C CA SER A 281 . 27.084 −14.628 6.092 1.00 34.89 . 1 1841 ATOM C C SER A 281 . 26.190 −13.681 5.308 1.00 35.50 . 1 1842 ATOM O O SER A 281 . 24.966 −13.703 5.452 1.00 34.38 . 1 1843 ATOM C CB SER A 281 . 27.751 −15.621 5.143 1.00 35.21 . 1 1844 ATOM O OG SER A 281 . 26.785 −16.457 4.529 1.00 36.68 . 1 1845 ATOM N N ASP A 282 . 26.812 −12.847 4.484 1.00 36.92 . 1 1846 ATOM C CA ASP A 282 . 26.083 −11.884 3.671 1.00 38.51 . 1 1847 ATOM C C ASP A 282 . 25.015 −12.554 2.816 1.00 38.65 . 1 1848 ATOM O O ASP A 282 . 23.855 −12.136 2.830 1.00 38.22 . 1 1849 ATOM C CB ASP A 282 . 27.058 −11.113 2.779 1.00 39.60 . 1 1850 ATOM C CG ASP A 282 . 27.872 −10.086 3.554 1.00 41.27 . 1 1851 ATOM O OD1 ASP A 282 . 28.006 −10.239 4.789 1.00 42.51 . 1 1852 ATOM O OD2 ASP A 282 . 28.390 −9.133 2.927 1.00 41.47 . 1 1853 ATOM N N GLU A 283 . 25.402 −13.593 2.083 1.00 39.78 . 1 1854 ATOM C CA GLU A 283 . 24.461 −14.305 1.217 1.00 40.55 . 1 1855 ATOM C C GLU A 283 . 23.180 −14.671 1.946 1.00 39.93 . 1 1856 ATOM O O GLU A 283 . 22.091 −14.246 1.566 1.00 40.02 . 1 1857 ATOM C CB GLU A 283 . 25.082 −15.593 0.674 1.00 42.54 . 1 1858 ATOM C CG GLU A 283 . 25.938 −15.433 −0.558 1.00 45.51 . 1 1859 ATOM C CD GLU A 283 . 26.386 −16.778 −1.113 1.00 47.63 . 1 1860 ATOM O OE1 GLU A 283 . 25.512 −17.621 −1.427 1.00 47.90 . 1 1861 ATOM O OE2 GLU A 283 . 27.611 −16.993 −1.235 1.00 48.98 . 1 1862 ATOM N N LYS A 284 . 23.324 −15.467 2.998 1.00 39.28 . 1 1863 ATOM C CA LYS A 284 . 22.186 −15.931 3.770 1.00 38.84 . 1 1864 ATOM C C LYS A 284 . 21.388 −14.808 4.423 1.00 38.31 . 1 1865 ATOM O O LYS A 284 . 20.164 −14.887 4.497 1.00 38.45 . 1 1866 ATOM C CB LYS A 284 . 22.659 −16.960 4.801 1.00 39.88 . 1 1867 ATOM C CG LYS A 284 . 23.417 −18.123 4.151 1.00 41.11 . 1 1868 ATOM C CD LYS A 284 . 23.907 −19.156 5.164 1.00 43.25 . 1 1869 ATOM C CE LYS A 284 . 24.754 −20.231 4.480 1.00 43.85 . 1 1870 ATOM N NZ LYS A 284 . 25.073 −21.371 5.391 1.00 45.22 . 1 1871 ATOM N N CYS A 285 . 22.064 −13.762 4.888 1.00 37.57 . 1 1872 ATOM C CA CYS A 285 . 21.363 −12.631 5.494 1.00 37.03 . 1 1873 ATOM C C CYS A 285 . 20.432 −11.992 4.463 1.00 36.91 . 1 1874 ATOM O O CYS A 285 . 19.257 −11.738 4.740 1.00 36.27 . 1 1875 ATOM C CB CYS A 285 . 22.354 −11.577 5.991 1.00 37.68 . 1 1876 ATOM S SG CYS A 285 . 23.057 −11.877 7.647 1.00 38.05 . 1 1877 ATOM N N ILE A 286 . 20.971 −11.714 3.281 1.00 36.71 . 1 1878 ATOM C CA ILE A 286 . 20.180 −11.110 2.209 1.00 36.91 . 1 1879 ATOM C C ILE A 286 . 18.979 −12.007 1.924 1.00 36.49 . 1 1880 ATOM O O ILE A 286 . 17.876 −11.530 1.678 1.00 36.71 . 1 1881 ATOM C CB ILE A 286 . 21.035 −10.936 0.934 1.00 37.36 . 1 1882 ATOM C CG1 ILE A 286 . 22.192 −9.976 1.228 1.00 37.23 . 1 1883 ATOM C CG2 ILE A 286 . 20.180 −10.391 −0.211 1.00 37.77 . 1 1884 ATOM C CD1 ILE A 286 . 23.311 −10.036 0.208 1.00 37.98 . 1 1885 ATOM N N GLU A 287 . 19.196 −13.313 1.982 1.00 36.87 . 1 1886 ATOM C CA GLU A 287 . 18.122 −14.267 1.753 1.00 37.28 . 1 1887 ATOM C C GLU A 287 . 16.924 −14.106 2.686 1.00 36.51 . 1 1888 ATOM O O GLU A 287 . 15.791 −13.957 2.217 1.00 35.98 . 1 1889 ATOM C CB GLU A 287 . 18.655 −15.693 1.856 1.00 39.29 . 1 1890 ATOM C CG GLU A 287 . 19.202 −16.246 0.548 1.00 42.68 . 1 1891 ATOM C CD GLU A 287 . 19.646 −17.689 0.688 1.00 44.26 . 1 1892 ATOM O OE1 GLU A 287 . 18.897 −18.460 1.325 1.00 45.76 . 1 1893 ATOM O OE2 GLU A 287 . 20.725 −18.049 0.164 1.00 45.00 . 1 1894 ATOM N N PHE A 288 . 17.136 −14.142 4.003 1.00 35.25 . 1 1895 ATOM C CA PHE A 288 . 15.981 −13.999 4.879 1.00 33.81 . 1 1896 ATOM C C PHE A 288 . 15.487 −12.561 5.012 1.00 33.29 . 1 1897 ATOM O O PHE A 288 . 14.310 −12.332 5.283 1.00 33.01 . 1 1898 ATOM C CB PHE A 288 . 16.213 −14.668 6.259 1.00 33.54 . 1 1899 ATOM C CG PHE A 288 . 17.405 −14.156 7.024 1.00 33.71 . 1 1900 ATOM C CD1 PHE A 288 . 17.389 −12.897 7.614 1.00 34.02 . 1 1901 ATOM C CD2 PHE A 288 . 18.523 −14.967 7.212 1.00 33.55 . 1 1902 ATOM C CE1 PHE A 288 . 18.470 −12.450 8.390 1.00 33.47 . 1 1903 ATOM C CE2 PHE A 288 . 19.610 −14.528 7.984 1.00 33.97 . 1 1904 ATOM C CZ PHE A 288 . 19.576 −13.264 8.573 1.00 33.06 . 1 1905 ATOM N N LEU A 289 . 16.363 −11.587 4.804 1.00 33.50 . 1 1906 ATOM C CA LEU A 289 . 15.921 −10.195 4.873 1.00 34.24 . 1 1907 ATOM C C LEU A 289 . 14.986 −9.908 3.688 1.00 34.78 . 1 1908 ATOM O O LEU A 289 . 14.002 −9.180 3.823 1.00 34.12 . 1 1909 ATOM C CB LEU A 289 . 17.114 −9.236 4.832 1.00 33.66 . 1 1910 ATOM C CG LEU A 289 . 17.981 −9.180 6.097 1.00 34.20 . 1 1911 ATOM C CD1 LEU A 289 . 19.222 −8.334 5.830 1.00 33.60 . 1 1912 ATOM C CD2 LEU A 289 . 17.164 −8.611 7.251 1.00 33.50 . 1 1913 ATOM N N SER A 290 . 15.299 −10.480 2.529 1.00 35.69 . 1 1914 ATOM C CA SER A 290 . 14.449 −10.289 1.352 1.00 37.22 . 1 1915 ATOM C C SER A 290 . 13.088 −10.904 1.643 1.00 37.40 . 1 1916 ATOM O O SER A 290 . 12.058 −10.333 1.299 1.00 37.75 . 1 1917 ATOM C CB SER A 290 . 15.074 −10.945 0.123 1.00 37.06 . 1 1918 ATOM O OG SER A 290 . 16.270 −10.279 −0.237 1.00 38.37 . 1 1919 ATOM N N ASN A 291 . 13.081 −12.070 2.287 1.00 37.91 . 1 1920 ATOM C CA ASN A 291 . 11.819 −12.710 2.634 1.00 38.23 . 1 1921 ATOM C C ASN A 291 . 11.051 −11.824 3.623 1.00 38.49 . 1 1922 ATOM O O ASN A 291 . 9.815 −11.776 3.600 1.00 38.58 . 1 1923 ATOM C CB ASN A 291 . 12.064 −14.107 3.224 1.00 38.66 . 1 1924 ATOM C CG ASN A 291 . 12.565 −15.102 2.176 1.00 39.39 . 1 1925 ATOM O OD1 ASN A 291 . 12.108 −15.087 1.034 1.00 39.75 . 1 1926 ATOM N ND2 ASN A 291 . 13.497 −15.974 2.565 1.00 38.95 . 1 1927 ATOM N N CYS A 292 . 11.782 −11.116 4.484 1.00 38.24 . 1 1928 ATOM C CA CYS A 292 . 11.147 −10.217 5.449 1.00 38.69 . 1 1929 ATOM C C CYS A 292 . 10.549 −9.032 4.688 1.00 39.26 . 1 1930 ATOM O O CYS A 292 . 9.490 −8.514 5.039 1.00 38.61 . 1 1931 ATOM C CB CYS A 292 . 12.167 −9.696 6.475 1.00 38.73 . 1 1932 ATOM S SG CYS A 292 . 12.634 −10.872 7.786 1.00 37.68 . 1 1933 ATOM N N HIS A 293 . 11.240 −8.603 3.640 1.00 40.04 . 1 1934 ATOM C CA HIS A 293 . 10.750 −7.493 2.841 1.00 41.20 . 1 1935 ATOM C C HIS A 293 . 9.428 −7.901 2.188 1.00 41.71 . 1 1936 ATOM O O HIS A 293 . 8.451 −7.155 2.238 1.00 41.88 . 1 1937 ATOM C CB HIS A 293 . 11.782 −7.116 1.780 1.00 41.86 . 1 1938 ATOM C CG HIS A 293 . 11.442 −5.870 1.026 1.00 43.30 . 1 1939 ATOM N ND1 HIS A 293 . 10.492 −5.839 0.028 1.00 43.71 . 1 1940 ATOM C CD2 HIS A 293 . 11.908 −4.604 1.141 1.00 43.25 . 1 1941 ATOM C CE1 HIS A 293 . 10.387 −4.608 −0.440 1.00 43.77 . 1 1942 ATOM N NE2 HIS A 293 . 11.236 −3.838 0.219 1.00 43.63 . 1 1943 ATOM N N LYS A 294 . 9.402 −9.095 1.598 1.00 42.12 . 1 1944 ATOM C CA LYS A 294 . 8.202 −9.610 0.943 1.00 43.49 . 1 1945 ATOM C C LYS A 294 . 6.988 −9.594 1.862 1.00 43.43 . 1 1946 ATOM O O LYS A 294 . 5.913 −9.134 1.472 1.00 43.62 . 1 1947 ATOM C CB LYS A 294 . 8.422 −11.052 0.465 1.00 44.65 . 1 1948 ATOM C CG LYS A 294 . 9.449 −11.216 −0.635 1.00 47.26 . 1 1949 ATOM C CD LYS A 294 . 9.648 −12.692 −0.984 1.00 49.39 . 1 1950 ATOM C CE LYS A 294 . 10.685 −12.868 −2.095 1.00 50.78 . 1 1951 ATOM N NZ LYS A 294 . 10.931 −14.302 −2.462 1.00 51.91 . 1 1952 ATOM N N ALA A 295 . 7.159 −10.095 3.085 1.00 42.93 . 1 1953 ATOM C CA ALA A 295 . 6.060 −10.172 4.037 1.00 41.88 . 1 1954 ATOM C C ALA A 295 . 5.728 −8.859 4.734 1.00 41.51 . 1 1955 ATOM O O ALA A 295 . 4.717 −8.761 5.428 1.00 41.58 . 1 1956 ATOM C CB ALA A 295 . 6.351 −11.261 5.074 1.00 42.43 . 1 1957 ATOM N N LEU A 296 . 6.569 −7.850 4.556 1.00 41.19 . 1 1958 ATOM C CA LEU A 296 . 6.324 −6.559 5.188 1.00 42.32 . 1 1959 ATOM C C LEU A 296 . 5.172 −5.815 4.532 1.00 43.31 . 1 1960 ATOM O O LEU A 296 . 5.004 −5.868 3.315 1.00 43.29 . 1 1961 ATOM C CB LEU A 296 . 7.568 −5.677 5.119 1.00 41.92 . 1 1962 ATOM C CG LEU A 296 . 8.431 −5.554 6.371 1.00 41.23 . 1 1963 ATOM C CD1 LEU A 296 . 9.582 −4.600 6.077 1.00 40.80 . 1 1964 ATOM C CD2 LEU A 296 . 7.593 −5.046 7.531 1.00 40.58 . 1 1965 ATOM N N SER A 297 . 4.388 −5.118 5.347 1.00 43.92 . 1 1966 ATOM C CA SER A 297 . 3.264 −4.341 4.846 1.00 44.77 . 1 1967 ATOM C C SER A 297 . 3.830 −3.222 3.978 1.00 45.38 . 1 1968 ATOM O O SER A 297 . 5.044 −3.012 3.944 1.00 45.50 . 1 1969 ATOM C CB SER A 297 . 2.478 −3.748 6.013 1.00 45.03 . 1 1970 ATOM O OG SER A 297 . 2.083 −4.766 6.912 1.00 47.02 . 1 1971 ATOM N N PRO A 298 . 2.957 −2.487 3.265 1.00 46.07 . 1 1972 ATOM C CA PRO A 298 . 3.362 −1.383 2.389 1.00 46.12 . 1 1973 ATOM C C PRO A 298 . 4.437 −0.450 2.949 1.00 45.95 . 1 1974 ATOM O O PRO A 298 . 5.522 −0.344 2.375 1.00 46.33 . 1 1975 ATOM C CB PRO A 298 . 2.041 −0.670 2.119 1.00 46.30 . 1 1976 ATOM C CG PRO A 298 . 1.096 −1.819 2.011 1.00 46.64 . 1 1977 ATOM C CD PRO A 298 . 1.496 −2.685 3.199 1.00 46.47 . 1 1978 ATOM N N ASN A 299 . 4.142 0.233 4.053 1.00 45.51 . 1 1979 ATOM C CA ASN A 299 . 5.118 1.143 4.648 1.00 45.25 . 1 1980 ATOM C C ASN A 299 . 5.688 0.585 5.959 1.00 44.47 . 1 1981 ATOM O O ASN A 299 . 5.832 1.309 6.948 1.00 43.86 . 1 1982 ATOM C CB ASN A 299 . 4.487 2.518 4.905 1.00 46.47 . 1 1983 ATOM C CG ASN A 299 . 3.883 3.130 3.648 1.00 47.36 . 1 1984 ATOM O OD1 ASN A 299 . 2.675 3.040 3.421 1.00 48.27 . 1 1985 ATOM N ND2 ASN A 299 . 4.725 3.744 2.821 1.00 47.16 . 1 1986 ATOM N N GLY A 300 . 6.011 −0.707 5.949 1.00 43.04 . 1 1987 ATOM C CA GLY A 300 . 6.556 −1.349 7.133 1.00 41.29 . 1 1988 ATOM C C GLY A 300 . 8.062 −1.201 7.246 1.00 40.20 . 1 1989 ATOM O O GLY A 300 . 8.722 −0.667 6.355 1.00 39.17 . 1 1990 ATOM N N LYS A 301 . 8.616 −1.678 8.354 1.00 38.96 . 1 1991 ATOM C CA LYS A 301 . 10.049 −1.585 8.564 1.00 38.12 . 1 1992 ATOM C C LYS A 301 . 10.588 −2.802 9.299 1.00 37.64 . 1 1993 ATOM O O LYS A 301 . 9.850 −3.511 9.988 1.00 37.35 . 1 1994 ATOM C CB LYS A 301 . 10.376 −0.330 9.375 1.00 38.60 . 1 1995 ATOM C CG LYS A 301 . 9.783 −0.347 10.769 1.00 38.24 . 1 1996 ATOM C CD LYS A 301 . 10.153 0.883 11.579 1.00 38.51 . 1 1997 ATOM C CE LYS A 301 . 9.415 0.857 12.909 1.00 39.11 . 1 1998 ATOM N NZ LYS A 301 . 9.719 2.030 13.768 1.00 38.09 . 1 1999 ATOM N N VAL A 302 . 11.879 −3.043 9.129 1.00 37.11 . 1 2000 ATOM C CA VAL A 302 . 12.553 −4.138 9.808 1.00 37.09 . 1 2001 ATOM C C VAL A 302 . 13.397 −3.489 10.898 1.00 36.50 . 1 2002 ATOM O O VAL A 302 . 14.055 −2.472 10.657 1.00 36.63 . 1 2003 ATOM C CB VAL A 302 . 13.485 −4.928 8.853 1.00 37.45 . 1 2004 ATOM C CG1 VAL A 302 . 14.499 −5.737 9.656 1.00 38.16 . 1 2005 ATOM C CG2 VAL A 302 . 12.667 −5.869 8.000 1.00 36.66 . 1 2006 ATOM N N ILE A 303 . 13.348 −4.050 12.102 1.00 34.92 . 1 2007 ATOM C CA ILE A 303 . 14.139 −3.520 13.199 1.00 33.77 . 1 2008 ATOM C C ILE A 303 . 15.240 −4.527 13.506 1.00 33.33 . 1 2009 ATOM O O ILE A 303 . 14.965 −5.690 13.801 1.00 32.81 . 1 2010 ATOM C CB ILE A 303 . 13.293 −3.296 14.459 1.00 33.52 . 1 2011 ATOM C CG1 ILE A 303 . 12.114 −2.374 14.144 1.00 32.95 . 1 2012 ATOM C CG2 ILE A 303 . 14.148 −2.658 15.543 1.00 33.81 . 1 2013 ATOM C CD1 ILE A 303 . 11.130 −2.241 15.283 1.00 32.35 . 1 2014 ATOM N N ILE A 304 . 16.484 −4.069 13.423 1.00 32.57 . 1 2015 ATOM C CA ILE A 304 . 17.649 −4.905 13.678 1.00 32.72 . 1 2016 ATOM C C ILE A 304 . 18.355 −4.461 14.961 1.00 31.96 . 1 2017 ATOM O O ILE A 304 . 18.750 −3.304 15.088 1.00 31.69 . 1 2018 ATOM C CB ILE A 304 . 18.658 −4.811 12.507 1.00 33.32 . 1 2019 ATOM C CG1 ILE A 304 . 17.976 −5.210 11.191 1.00 33.99 . 1 2020 ATOM C CG2 ILE A 304 . 19.851 −5.724 12.761 1.00 33.58 . 1 2021 ATOM C CD1 ILE A 304 . 17.509 −6.659 11.146 1.00 34.02 . 1 2022 ATOM N N VAL A 305 . 18.504 −5.378 15.912 1.00 31.02 . 1 2023 ATOM C CA VAL A 305 . 19.181 −5.067 17.166 1.00 30.15 . 1 2024 ATOM C C VAL A 305 . 20.479 −5.869 17.217 1.00 30.55 . 1 2025 ATOM O O VAL A 305 . 20.474 −7.072 17.502 1.00 29.28 . 1 2026 ATOM C CB VAL A 305 . 18.293 −5.407 18.391 1.00 30.05 . 1 2027 ATOM C CG1 VAL A 305 . 19.017 −5.023 19.693 1.00 29.88 . 1 2028 ATOM C CG2 VAL A 305 . 16.965 −4.650 18.298 1.00 29.44 . 1 2029 ATOM N N GLU A 306 . 21.585 −5.185 16.930 1.00 30.39 . 1 2030 ATOM C CA GLU A 306 . 22.911 −5.789 16.901 1.00 31.83 . 1 2031 ATOM C C GLU A 306 . 23.960 −4.799 17.388 1.00 31.92 . 1 2032 ATOM O O GLU A 306 . 23.720 −3.593 17.404 1.00 32.13 . 1 2033 ATOM C CB GLU A 306 . 23.271 −6.203 15.466 1.00 32.98 . 1 2034 ATOM C CG GLU A 306 . 22.461 −7.374 14.913 1.00 35.81 . 1 2035 ATOM C CD GLU A 306 . 23.080 −8.718 15.249 1.00 37.28 . 1 2036 ATOM O OE1 GLU A 306 . 23.948 −8.760 16.146 1.00 38.63 . 1 2037 ATOM O OE2 GLU A 306 . 22.699 −9.731 14.626 1.00 37.55 . 1 2038 ATOM N N PHE A 307 . 25.123 −5.309 17.786 1.00 31.71 . 1 2039 ATOM C CA PHE A 307 . 26.199 −4.431 18.206 1.00 31.88 . 1 2040 ATOM C C PHE A 307 . 26.821 −3.881 16.935 1.00 32.64 . 1 2041 ATOM O O PHE A 307 . 26.907 −4.575 15.923 1.00 31.47 . 1 2042 ATOM C CB PHE A 307 . 27.254 −5.179 19.024 1.00 32.29 . 1 2043 ATOM C CG PHE A 307 . 26.842 −5.428 20.445 1.00 31.73 . 1 2044 ATOM C CD1 PHE A 307 . 26.204 −6.600 20.799 1.00 31.43 . 1 2045 ATOM C CD2 PHE A 307 . 27.051 −4.455 21.418 1.00 32.12 . 1 2046 ATOM C CE1 PHE A 307 . 25.774 −6.811 22.103 1.00 32.98 . 1 2047 ATOM C CE2 PHE A 307 . 26.624 −4.655 22.730 1.00 32.44 . 1 2048 ATOM C CZ PHE A 307 . 25.982 −5.838 23.071 1.00 31.92 . 1 2049 ATOM N N ILE A 308 . 27.254 −2.632 16.981 1.00 32.48 . 1 2050 ATOM C CA ILE A 308 . 27.840 −2.034 15.799 1.00 33.72 . 1 2051 ATOM C C ILE A 308 . 29.349 −1.856 15.889 1.00 33.78 . 1 2052 ATOM O O ILE A 308 . 29.848 −1.165 16.774 1.00 33.93 . 1 2053 ATOM C CB ILE A 308 . 27.184 −0.669 15.507 1.00 34.05 . 1 2054 ATOM C CG1 ILE A 308 . 25.667 −0.852 15.385 1.00 34.17 . 1 2055 ATOM C CG2 ILE A 308 . 27.754 −0.078 14.223 1.00 35.09 . 1 2056 ATOM C CD1 ILE A 308 . 24.891 0.435 15.248 1.00 33.31 . 1 2057 ATOM N N LEU A 309 . 30.064 −2.504 14.974 1.00 33.07 . 1 2058 ATOM C CA LEU A 309 . 31.510 −2.393 14.896 1.00 34.35 . 1 2059 ATOM C C LEU A 309 . 31.838 −1.008 14.354 1.00 34.78 . 1 2060 ATOM O O LEU A 309 . 31.254 −0.581 13.353 1.00 33.56 . 1 2061 ATOM C CB LEU A 309 . 32.079 −3.413 13.906 1.00 35.21 . 1 2062 ATOM C CG LEU A 309 . 32.642 −4.770 14.326 1.00 36.78 . 1 2063 ATOM C CD1 LEU A 309 . 33.013 −5.560 13.058 1.00 37.52 . 1 2064 ATOM C CD2 LEU A 309 . 33.865 −4.585 15.216 1.00 36.47 . 1 2065 ATOM N N PRO A 310 . 32.760 −0.279 15.003 1.00 35.30 . 1 2066 ATOM C CA PRO A 310 . 33.073 1.049 14.453 1.00 35.20 . 1 2067 ATOM C C PRO A 310 . 33.719 0.890 13.077 1.00 35.17 . 1 2068 ATOM O O PRO A 310 . 34.369 −0.117 12.797 1.00 34.90 . 1 2069 ATOM C CB PRO A 310 . 34.016 1.654 15.495 1.00 35.53 . 1 2070 ATOM C CG PRO A 310 . 34.616 0.443 16.178 1.00 36.24 . 1 2071 ATOM C CD PRO A 310 . 33.428 −0.488 16.298 1.00 35.54 . 1 2072 ATOM N N GLU A 311 . 33.513 1.873 12.208 1.00 35.85 . 1 2073 ATOM C CA GLU A 311 . 34.057 1.825 10.853 1.00 35.64 . 1 2074 ATOM C C GLU A 311 . 35.526 1.424 10.884 1.00 35.32 . 1 2075 ATOM O O GLU A 311 . 35.968 0.553 10.129 1.00 34.81 . 1 2076 ATOM C CB GLU A 311 . 33.887 3.190 10.180 1.00 37.13 . 1 2077 ATOM C CG GLU A 311 . 34.178 3.194 8.691 1.00 39.65 . 1 2078 ATOM C CD GLU A 311 . 33.427 2.106 7.949 1.00 40.99 . 1 2079 ATOM O OE1 GLU A 311 . 32.237 1.870 8.260 1.00 42.53 . 1 2080 ATOM O OE2 GLU A 311 . 34.032 1.493 7.044 1.00 42.75 . 1 2081 ATOM N N GLU A 312 . 36.284 2.073 11.759 1.00 34.90 . 1 2082 ATOM C CA GLU A 312 . 37.694 1.772 11.920 1.00 34.79 . 1 2083 ATOM C C GLU A 312 . 37.935 1.478 13.398 1.00 33.95 . 1 2084 ATOM O O GLU A 312 . 37.247 2.013 14.260 1.00 33.25 . 1 2085 ATOM C CB GLU A 312 . 38.550 2.960 11.471 1.00 36.68 . 1 2086 ATOM C CG GLU A 312 . 38.469 3.269 9.977 1.00 37.84 . 1 2087 ATOM C CD GLU A 312 . 38.884 2.093 9.108 1.00 38.84 . 1 2088 ATOM O OE1 GLU A 312 . 39.842 1.387 9.480 1.00 38.54 . 1 2089 ATOM O OE2 GLU A 312 . 38.259 1.880 8.043 1.00 40.51 . 1 2090 ATOM N N PRO A 313 . 38.902 0.607 13.710 1.00 33.71 . 1 2091 ATOM C CA PRO A 313 . 39.140 0.320 15.127 1.00 33.58 . 1 2092 ATOM C C PRO A 313 . 39.794 1.485 15.852 1.00 33.41 . 1 2093 ATOM O O PRO A 313 . 40.602 2.211 15.277 1.00 33.11 . 1 2094 ATOM C CB PRO A 313 . 40.036 −0.915 15.081 1.00 33.84 . 1 2095 ATOM C CG PRO A 313 . 40.805 −0.722 13.803 1.00 33.73 . 1 2096 ATOM C CD PRO A 313 . 39.733 −0.252 12.851 1.00 33.05 . 1 2097 ATOM N N ASN A 314 . 39.424 1.669 17.112 1.00 32.79 . 1 2098 ATOM C CA ASN A 314 . 40.004 2.721 17.927 1.00 33.53 . 1 2099 ATOM C C ASN A 314 . 40.143 2.204 19.354 1.00 33.28 . 1 2100 ATOM O O ASN A 314 . 39.867 1.038 19.628 1.00 32.59 . 1 2101 ATOM C CB ASN A 314 . 39.142 3.986 17.899 1.00 33.27 . 1 2102 ATOM C CG ASN A 314 . 37.700 3.713 18.228 1.00 33.62 . 1 2103 ATOM O OD1 ASN A 314 . 36.862 3.623 17.338 1.00 35.35 . 1 2104 ATOM N ND2 ASN A 314 . 37.399 3.561 19.511 1.00 32.87 . 1 2105 ATOM N N THR A 315 . 40.545 3.077 20.268 1.00 33.05 . 1 2106 ATOM C CA THR A 315 . 40.751 2.664 21.649 1.00 32.51 . 1 2107 ATOM C C THR A 315 . 39.584 2.905 22.600 1.00 32.11 . 1 2108 ATOM O O THR A 315 . 39.762 2.885 23.820 1.00 32.08 . 1 2109 ATOM C CB THR A 315 . 42.011 3.333 22.218 1.00 32.62 . 1 2110 ATOM O OG1 THR A 315 . 41.842 4.754 22.204 1.00 33.46 . 1 2111 ATOM C CG2 THR A 315 . 43.216 2.974 21.372 1.00 31.68 . 1 2112 ATOM N N SER A 316 . 38.391 3.120 22.058 1.00 31.57 . 1 2113 ATOM C CA SER A 316 . 37.219 3.327 22.899 1.00 31.32 . 1 2114 ATOM C C SER A 316 . 36.742 1.982 23.447 1.00 31.25 . 1 2115 ATOM O O SER A 316 . 37.113 0.925 22.941 1.00 29.77 . 1 2116 ATOM C CB SER A 316 . 36.077 3.952 22.105 1.00 32.09 . 1 2117 ATOM O OG SER A 316 . 35.504 3.005 21.218 1.00 32.36 . 1 2118 ATOM N N GLU A 317 . 35.912 2.047 24.479 1.00 31.39 . 1 2119 ATOM C CA GLU A 317 . 35.347 0.864 25.123 1.00 32.69 . 1 2120 ATOM C C GLU A 317 . 34.455 0.079 24.158 1.00 31.75 . 1 2121 ATOM O O GLU A 317 . 34.419 −1.154 24.201 1.00 30.70 . 1 2122 ATOM C CB GLU A 317 . 34.518 1.290 26.339 1.00 34.60 . 1 2123 ATOM C CG GLU A 317 . 35.046 0.808 27.671 1.00 38.77 . 1 2124 ATOM C CD GLU A 317 . 36.528 1.007 27.796 1.00 40.69 . 1 2125 ATOM O OE1 GLU A 317 . 36.994 2.145 27.571 1.00 43.49 . 1 2126 ATOM O OE2 GLU A 317 . 37.234 0.028 28.113 1.00 41.35 . 1 2127 ATOM N N GLU A 318 . 33.720 0.790 23.306 1.00 30.64 . 1 2128 ATOM C CA GLU A 318 . 32.841 0.118 22.357 1.00 30.78 . 1 2129 ATOM C C GLU A 318 . 33.635 −0.641 21.309 1.00 29.46 . 1 2130 ATOM O O GLU A 318 . 33.213 −1.714 20.868 1.00 29.77 . 1 2131 ATOM C CB GLU A 318 . 31.894 1.105 21.665 1.00 33.11 . 1 2132 ATOM C CG GLU A 318 . 32.556 2.241 20.930 1.00 36.84 . 1 2133 ATOM C CD GLU A 318 . 32.748 3.459 21.812 1.00 38.72 . 1 2134 ATOM O OE1 GLU A 318 . 33.064 4.544 21.266 1.00 41.16 . 1 2135 ATOM O OE2 GLU A 318 . 32.581 3.334 23.050 1.00 41.63 . 1 2136 ATOM N N SER A 319 . 34.777 −0.093 20.901 1.00 27.66 . 1 2137 ATOM C CA SER A 319 . 35.609 −0.765 19.915 1.00 27.13 . 1 2138 ATOM C C SER A 319 . 36.166 −2.031 20.573 1.00 26.70 . 1 2139 ATOM O O SER A 319 . 36.233 −3.091 19.955 1.00 25.84 . 1 2140 ATOM C CB SER A 319 . 36.756 0.142 19.444 1.00 25.77 . 1 2141 ATOM O OG SER A 319 . 37.529 −0.495 18.429 1.00 25.48 . 1 2142 ATOM N N LYS A 320 . 36.562 −1.915 21.837 1.00 26.66 . 1 2143 ATOM C CA LYS A 320 . 37.086 −3.073 22.569 1.00 26.56 . 1 2144 ATOM C C LYS A 320 . 36.002 −4.133 22.697 1.00 25.83 . 1 2145 ATOM O O LYS A 320 . 36.249 −5.314 22.435 1.00 26.30 . 1 2146 ATOM C CB LYS A 320 . 37.549 −2.666 23.975 1.00 26.70 . 1 2147 ATOM C CG LYS A 320 . 38.860 −1.914 24.017 1.00 28.43 . 1 2148 ATOM C CD LYS A 320 . 39.053 −1.237 25.369 1.00 30.09 . 1 2149 ATOM C CE LYS A 320 . 40.344 −0.434 25.403 1.00 31.50 . 1 2150 ATOM N NZ LYS A 320 . 40.467 0.334 26.673 1.00 32.77 . 1 2151 ATOM N N LEU A 321 . 34.800 −3.716 23.085 1.00 25.45 . 1 2152 ATOM C CA LEU A 321 . 33.706 −4.662 23.259 1.00 24.80 . 1 2153 ATOM C C LEU A 321 . 33.276 −5.368 21.990 1.00 25.31 . 1 2154 ATOM O O LEU A 321 . 33.304 −6.592 21.930 1.00 23.74 . 1 2155 ATOM C CB LEU A 321 . 32.469 −3.999 23.870 1.00 24.90 . 1 2156 ATOM C CG LEU A 321 . 31.300 −4.995 24.020 1.00 24.35 . 1 2157 ATOM C CD1 LEU A 321 . 31.664 −6.045 25.087 1.00 24.88 . 1 2158 ATOM C CD2 LEU A 321 . 30.011 −4.277 24.410 1.00 24.27 . 1 2159 ATOM N N VAL A 322 . 32.869 −4.598 20.981 1.00 25.55 . 1 2160 ATOM C CA VAL A 322 . 32.398 −5.198 19.734 1.00 25.55 . 1 2161 ATOM C C VAL A 322 . 33.468 −6.038 19.061 1.00 25.36 . 1 2162 ATOM O O VAL A 322 . 33.155 −7.073 18.486 1.00 26.37 . 1 2163 ATOM C CB VAL A 322 . 31.831 −4.127 18.761 1.00 25.22 . 1 2164 ATOM C CG1 VAL A 322 . 31.108 −4.819 17.578 1.00 25.92 . 1 2165 ATOM C CG2 VAL A 322 . 30.837 −3.240 19.499 1.00 25.53 . 1 2166 ATOM N N SER A 323 . 34.727 −5.616 19.110 1.00 25.36 . 1 2167 ATOM C CA SER A 323 . 35.780 −6.436 18.531 1.00 26.04 . 1 2168 ATOM C C SER A 323 . 35.947 −7.743 19.330 1.00 25.96 . 1 2169 ATOM O O SER A 323 . 36.310 −8.778 18.769 1.00 26.57 . 1 2170 ATOM C CB SER A 323 . 37.109 −5.683 18.488 1.00 26.74 . 1 2171 ATOM O OG SER A 323 . 37.181 −4.904 17.309 1.00 31.33 . 1 2172 ATOM N N THR A 324 . 35.685 −7.695 20.630 1.00 25.09 . 1 2173 ATOM C CA THR A 324 . 35.791 −8.902 21.469 1.00 25.19 . 1 2174 ATOM C C THR A 324 . 34.667 −9.880 21.125 1.00 25.83 . 1 2175 ATOM O O THR A 324 . 34.895 −11.087 21.020 1.00 25.31 . 1 2176 ATOM C CB THR A 324 . 35.721 −8.549 22.979 1.00 23.99 . 1 2177 ATOM O OG1 THR A 324 . 36.919 −7.871 23.351 1.00 23.41 . 1 2178 ATOM C CG2 THR A 324 . 35.590 −9.810 23.839 1.00 24.25 . 1 2179 ATOM N N LEU A 325 . 33.458 −9.355 20.944 1.00 26.99 . 1 2180 ATOM C CA LEU A 325 . 32.316 −10.191 20.593 1.00 28.58 . 1 2181 ATOM C C LEU A 325 . 32.554 −10.820 19.223 1.00 29.37 . 1 2182 ATOM O O LEU A 325 . 32.266 −12.000 19.007 1.00 29.39 . 1 2183 ATOM C CB LEU A 325 . 31.026 −9.361 20.574 1.00 28.78 . 1 2184 ATOM C CG LEU A 325 . 30.560 −8.822 21.931 1.00 30.91 . 1 2185 ATOM C CD1 LEU A 325 . 29.309 −7.957 21.766 1.00 30.22 . 1 2186 ATOM C CD2 LEU A 325 . 30.268 −9.990 22.867 1.00 31.18 . 1 2187 ATOM N N ASP A 326 . 33.090 −10.027 18.302 1.00 30.56 . 1 2188 ATOM C CA ASP A 326 . 33.383 −10.505 16.960 1.00 32.44 . 1 2189 ATOM C C ASP A 326 . 34.301 −11.730 16.997 1.00 33.03 . 1 2190 ATOM O O ASP A 326 . 34.067 −12.711 16.287 1.00 33.05 . 1 2191 ATOM C CB ASP A 326 . 34.032 −9.394 16.137 1.00 33.57 . 1 2192 ATOM C CG ASP A 326 . 34.131 −9.747 14.665 1.00 34.81 . 1 2193 ATOM O OD1 ASP A 326 . 33.190 −10.379 14.145 1.00 34.89 . 1 2194 ATOM O OD2 ASP A 326 . 35.141 −9.385 14.028 1.00 37.60 . 1 2195 ATOM N N ASN A 327 . 35.340 −11.677 17.824 1.00 33.22 . 1 2196 ATOM C CA ASN A 327 . 36.261 −12.803 17.940 1.00 34.11 . 1 2197 ATOM C C ASN A 327 . 35.592 −13.975 18.646 1.00 35.01 . 1 2198 ATOM O O ASN A 327 . 35.869 −15.140 18.346 1.00 34.87 . 1 2199 ATOM C CB ASN A 327 . 37.523 −12.367 18.682 1.00 33.78 . 1 2200 ATOM C CG ASN A 327 . 38.472 −11.600 17.791 1.00 33.82 . 1 2201 ATOM O OD1 ASN A 327 . 39.273 −12.191 17.074 1.00 33.54 . 1 2202 ATOM N ND2 ASN A 327 . 38.367 −10.275 17.810 1.00 33.57 . 1 2203 ATOM N N LEU A 328 . 34.699 −13.659 19.574 1.00 36.26 . 1 2204 ATOM C CA LEU A 328 . 33.966 −14.678 20.309 1.00 38.62 . 1 2205 ATOM C C LEU A 328 . 33.017 −15.418 19.349 1.00 39.84 . 1 2206 ATOM O O LEU A 328 . 32.947 −16.647 19.363 1.00 40.38 . 1 2207 ATOM C CB LEU A 328 . 33.183 −14.019 21.451 1.00 37.86 . 1 2208 ATOM C CG LEU A 328 . 32.567 −14.895 22.550 1.00 39.23 . 1 2209 ATOM C CD1 LEU A 328 . 32.281 −14.046 23.781 1.00 38.53 . 1 2210 ATOM C CD2 LEU A 328 . 31.295 −15.557 22.050 1.00 38.39 . 1 2211 HETA N N MSE A 329 . 32.304 −14.663 18.514 1.00 41.79 . 1 2212 HETA C CA MSE A 329 . 31.365 −15.239 17.549 1.00 44.16 . 1 2213 HETA C C MSE A 329 . 32.090 −16.151 16.586 1.00 46.07 . 1 2214 HETA O O MSE A 329 . 31.661 −17.273 16.332 1.00 46.96 . 1 2215 HETA C CB MSE A 329 . 30.653 −14.145 16.744 1.00 43.18 . 1 2216 HETA C CG MSE A 329 . 29.621 −13.355 17.516 1.00 43.00 . 1 2217 HETA SE SE MSE A 329 . 28.313 −14.377 18.215 1.00 42.26 . 1 2218 HETA C CE MSE A 329 . 28.749 −14.380 19.927 1.00 40.55 . 1 2219 ATOM N N PHE A 330 . 33.192 −15.656 16.041 1.00 48.69 . 1 2220 ATOM C CA PHE A 330 . 33.984 −16.430 15.105 1.00 51.48 . 1 2221 ATOM C C PHE A 330 . 34.371 −17.794 15.660 1.00 53.11 . 1 2222 ATOM O O PHE A 330 . 33.980 −18.825 15.123 1.00 54.00 . 1 2223 ATOM C CB PHE A 330 . 35.243 −15.650 14.721 1.00 51.59 . 1 2224 ATOM C CG PHE A 330 . 36.336 −16.504 14.146 1.00 51.61 . 1 2225 ATOM C CD1 PHE A 330 . 37.443 −16.850 14.917 1.00 51.84 . 1 2226 ATOM C CD2 PHE A 330 . 36.256 −16.970 12.838 1.00 51.55 . 1 2227 ATOM C CE1 PHE A 330 . 38.459 −17.650 14.391 1.00 51.88 . 1 2228 ATOM C CE2 PHE A 330 . 37.264 −17.770 12.303 1.00 51.85 . 1 2229 ATOM C CZ PHE A 330 . 38.368 −18.110 13.079 1.00 52.25 . 1 2230 ATOM N N ILE A 331 . 35.137 −17.802 16.740 1.00 54.88 . 1 2231 ATOM C CA ILE A 331 . 35.582 −19.058 17.323 1.00 56.79 . 1 2232 ATOM C C ILE A 331 . 34.422 −19.964 17.735 1.00 57.54 . 1 2233 ATOM O O ILE A 331 . 34.520 −21.186 17.633 1.00 58.43 . 1 2234 ATOM C CB ILE A 331 . 36.499 −18.808 18.544 1.00 57.42 . 1 2235 ATOM C CG1 ILE A 331 . 37.125 −20.127 19.003 1.00 57.70 . 1 2236 ATOM C CG2 ILE A 331 . 35.707 −18.166 19.669 1.00 57.68 . 1 2237 ATOM C CD1 ILE A 331 . 38.040 −19.984 20.199 1.00 57.81 . 1 2238 ATOM N N THR A 332 . 33.324 −19.366 18.186 1.00 58.22 . 1 2239 ATOM C CA THR A 332 . 32.156 −20.130 18.616 1.00 59.10 . 1 2240 ATOM C C THR A 332 . 31.286 −20.599 17.447 1.00 59.50 . 1 2241 ATOM O O THR A 332 . 30.750 −21.708 17.471 1.00 60.21 . 1 2242 ATOM C CB THR A 332 . 31.282 −19.301 19.598 1.00 59.50 . 1 2243 ATOM O OG1 THR A 332 . 31.917 −19.255 20.882 1.00 59.01 . 1 2244 ATOM C CG2 THR A 332 . 29.899 −19.912 19.750 1.00 59.86 . 1 2245 ATOM N N VAL A 333 . 31.146 −19.752 16.432 1.00 59.65 . 1 2246 ATOM C CA VAL A 333 . 30.336 −20.067 15.258 1.00 59.80 . 1 2247 ATOM C C VAL A 333 . 30.888 −19.342 14.030 1.00 59.42 . 1 2248 ATOM O O VAL A 333 . 31.857 −18.595 14.124 1.00 59.88 . 1 2249 ATOM C CB VAL A 333 . 28.870 −19.618 15.455 1.00 60.44 . 1 2250 ATOM C CG1 VAL A 333 . 28.003 −20.155 14.323 1.00 60.84 . 1 2251 ATOM C CG2 VAL A 333 . 28.350 −20.093 16.800 1.00 61.15 . 1 2252 ATOM N N GLY A 334 . 30.269 −19.561 12.876 1.00 58.78 . 1 2253 ATOM C CA GLY A 334 . 30.723 −18.895 11.669 1.00 57.06 . 1 2254 ATOM C C GLY A 334 . 30.175 −17.484 11.623 1.00 55.75 . 1 2255 ATOM O O GLY A 334 . 30.065 −16.886 10.554 1.00 56.93 . 1 2256 ATOM N N GLY A 335 . 29.836 −16.949 12.795 1.00 53.61 . 1 2257 ATOM C CA GLY A 335 . 29.285 −15.610 12.870 1.00 50.61 . 1 2258 ATOM C C GLY A 335 . 30.322 −14.507 12.926 1.00 48.60 . 1 2259 ATOM O O GLY A 335 . 31.518 −14.765 13.023 1.00 48.42 . 1 2260 ATOM N N ARG A 336 . 29.852 −13.267 12.851 1.00 45.75 . 1 2261 ATOM C CA ARG A 336 . 30.728 −12.111 12.910 1.00 43.74 . 1 2262 ATOM C C ARG A 336 . 29.895 −10.868 13.167 1.00 41.27 . 1 2263 ATOM O O ARG A 336 . 28.691 −10.856 12.927 1.00 41.24 . 1 2264 ATOM C CB ARG A 336 . 31.507 −11.938 11.597 1.00 45.28 . 1 2265 ATOM C CG ARG A 336 . 30.780 −11.149 10.501 1.00 47.50 . 1 2266 ATOM C CD ARG A 336 . 30.208 −12.064 9.434 1.00 49.52 . 1 2267 ATOM N NE ARG A 336 . 29.258 −13.009 10.003 1.00 51.32 . 1 2268 ATOM C CZ ARG A 336 . 29.057 −14.237 9.538 1.00 53.00 . 1 2269 ATOM N NH1 ARG A 336 . 29.740 −14.675 8.488 1.00 53.37 . 1 2270 ATOM N NH2 ARG A 336 . 28.187 −15.036 10.139 1.00 54.50 . 1 2271 ATOM N N GLU A 337 . 30.541 −9.828 13.673 1.00 38.67 . 1 2272 ATOM C CA GLU A 337 . 29.858 −8.576 13.930 1.00 36.64 . 1 2273 ATOM C C GLU A 337 . 30.054 −7.735 12.680 1.00 34.97 . 1 2274 ATOM O O GLU A 337 . 30.938 −8.019 11.882 1.00 34.79 . 1 2275 ATOM C CB GLU A 337 . 30.451 −7.884 15.158 1.00 37.66 . 1 2276 ATOM C CG GLU A 337 . 30.207 −8.640 16.467 1.00 38.92 . 1 2277 ATOM C CD GLU A 337 . 28.773 −9.133 16.608 1.00 40.50 . 1 2278 ATOM O OE1 GLU A 337 . 27.832 −8.318 16.486 1.00 41.60 . 1 2279 ATOM O OE2 GLU A 337 . 28.582 −10.347 16.845 1.00 42.74 . 1 2280 ATOM N N ARG A 338 . 29.236 −6.708 12.505 1.00 33.61 . 1 2281 ATOM C CA ARG A 338 . 29.337 −5.873 11.310 1.00 32.64 . 1 2282 ATOM C C ARG A 338 . 29.299 −4.383 11.613 1.00 31.38 . 1 2283 ATOM O O ARG A 338 . 28.753 −3.960 12.635 1.00 31.16 . 1 2284 ATOM C CB ARG A 338 . 28.189 −6.200 10.341 1.00 31.88 . 1 2285 ATOM C CG ARG A 338 . 28.246 −7.580 9.688 1.00 31.49 . 1 2286 ATOM C CD ARG A 338 . 27.018 −7.801 8.799 1.00 30.05 . 1 2287 ATOM N NE ARG A 338 . 27.147 −8.948 7.901 1.00 29.83 . 1 2288 ATOM C CZ ARG A 338 . 26.733 −10.183 8.187 1.00 30.01 . 1 2289 ATOM N NH1 ARG A 338 . 26.158 −10.454 9.355 1.00 27.56 . 1 2290 ATOM N NH2 ARG A 338 . 26.883 −11.149 7.293 1.00 30.40 . 1 2291 ATOM N N THR A 339 . 29.872 −3.599 10.704 1.00 30.79 . 1 2292 ATOM C CA THR A 339 . 29.889 −2.148 10.836 1.00 30.90 . 1 2293 ATOM C C THR A 339 . 28.523 −1.625 10.419 1.00 31.57 . 1 2294 ATOM O O THR A 339 . 27.688 −2.370 9.898 1.00 31.50 . 1 2295 ATOM C CB THR A 339 . 30.921 −1.476 9.894 1.00 30.08 . 1 2296 ATOM O OG1 THR A 339 . 30.605 −1.818 8.539 1.00 30.48 . 1 2297 ATOM C CG2 THR A 339 . 32.347 −1.923 10.212 1.00 28.67 . 1 2298 ATOM N N GLU A 340 . 28.306 −0.338 10.653 1.00 31.98 . 1 2299 ATOM C CA GLU A 340 . 27.053 0.304 10.292 1.00 33.73 . 1 2300 ATOM C C GLU A 340 . 26.884 0.285 8.774 1.00 33.94 . 1 2301 ATOM O O GLU A 340 . 25.792 0.062 8.268 1.00 34.37 . 1 2302 ATOM C CB GLU A 340 . 27.043 1.755 10.776 1.00 35.10 . 1 2303 ATOM C CG GLU A 340 . 25.732 2.471 10.517 1.00 38.18 . 1 2304 ATOM C CD GLU A 340 . 25.796 3.951 10.838 1.00 40.14 . 1 2305 ATOM O OE1 GLU A 340 . 26.324 4.304 11.918 1.00 42.25 . 1 2306 ATOM O OE2 GLU A 340 . 25.309 4.758 10.015 1.00 40.85 . 1 2307 ATOM N N LYS A 341 . 27.974 0.526 8.053 1.00 34.38 . 1 2308 ATOM C CA LYS A 341 . 27.926 0.544 6.598 1.00 35.03 . 1 2309 ATOM C C LYS A 341 . 27.637 −0.829 6.022 1.00 34.71 . 1 2310 ATOM O O LYS A 341 . 26.991 −0.945 4.983 1.00 34.10 . 1 2311 ATOM C CB LYS A 341 . 29.235 1.080 6.025 1.00 36.53 . 1 2312 ATOM C CG LYS A 341 . 29.422 2.562 6.246 1.00 38.66 . 1 2313 ATOM C CD LYS A 341 . 30.718 3.046 5.625 1.00 41.18 . 1 2314 ATOM C CE LYS A 341 . 30.922 4.529 5.886 1.00 41.78 . 1 2315 ATOM N NZ LYS A 341 . 32.247 4.980 5.374 1.00 43.70 . 1 2316 ATOM N N GLN A 342 . 28.104 −1.874 6.698 1.00 33.75 . 1 2317 ATOM C CA GLN A 342 . 27.860 −3.225 6.208 1.00 33.56 . 1 2318 ATOM C C GLN A 342 . 26.405 −3.630 6.388 1.00 33.74 . 1 2319 ATOM O O GLN A 342 . 25.872 −4.387 5.584 1.00 34.04 . 1 2320 ATOM C CB GLN A 342 . 28.785 −4.222 6.896 1.00 33.05 . 1 2321 ATOM C CG GLN A 342 . 30.237 −4.052 6.500 1.00 33.48 . 1 2322 ATOM C CD GLN A 342 . 31.172 −4.967 7.278 1.00 34.46 . 1 2323 ATOM O OE1 GLN A 342 . 31.074 −5.079 8.503 1.00 33.37 . 1 2324 ATOM N NE2 GLN A 342 . 32.091 −5.613 6.570 1.00 34.88 . 1 2325 ATOM N N TYR A 343 . 25.758 −3.128 7.437 1.00 34.13 . 1 2326 ATOM C CA TYR A 343 . 24.352 −3.441 7.664 1.00 34.59 . 1 2327 ATOM C C TYR A 343 . 23.490 −2.676 6.663 1.00 35.39 . 1 2328 ATOM O O TYR A 343 . 22.460 −3.171 6.210 1.00 34.51 . 1 2329 ATOM C CB TYR A 343 . 23.925 −3.067 9.087 1.00 34.14 . 1 2330 ATOM C CG TYR A 343 . 24.247 −4.126 10.124 1.00 32.93 . 1 2331 ATOM C CD1 TYR A 343 . 25.180 −3.888 11.133 1.00 32.70 . 1 2332 ATOM C CD2 TYR A 343 . 23.614 −5.373 10.086 1.00 33.90 . 1 2333 ATOM C CE1 TYR A 343 . 25.479 −4.872 12.087 1.00 32.34 . 1 2334 ATOM C CE2 TYR A 343 . 23.905 −6.365 11.034 1.00 33.29 . 1 2335 ATOM C CZ TYR A 343 . 24.834 −6.110 12.026 1.00 32.81 . 1 2336 ATOM O OH TYR A 343 . 25.123 −7.099 12.945 1.00 33.70 . 1 2337 ATOM N N GLU A 344 . 23.907 −1.461 6.329 1.00 36.45 . 1 2338 ATOM C CA GLU A 344 . 23.154 −0.672 5.364 1.00 38.43 . 1 2339 ATOM C C GLU A 344 . 23.242 −1.351 3.998 1.00 38.35 . 1 2340 ATOM O O GLU A 344 . 22.271 −1.394 3.247 1.00 38.51 . 1 2341 ATOM C CB GLU A 344 . 23.712 0.745 5.285 1.00 39.68 . 1 2342 ATOM C CG GLU A 344 . 22.862 1.674 4.446 1.00 42.63 . 1 2343 ATOM C CD GLU A 344 . 23.372 3.095 4.473 1.00 43.88 . 1 2344 ATOM O OE1 GLU A 344 . 22.625 4.002 4.044 1.00 46.07 . 1 2345 ATOM O OE2 GLU A 344 . 24.520 3.306 4.919 1.00 44.64 . 1 2346 ATOM N N LYS A 345 . 24.414 −1.888 3.690 1.00 39.23 . 1 2347 ATOM C CA LYS A 345 . 24.633 −2.587 2.431 1.00 40.54 . 1 2348 ATOM C C LYS A 345 . 23.645 −3.749 2.351 1.00 41.13 . 1 2349 ATOM O O LYS A 345 . 22.997 −3.972 1.323 1.00 41.46 . 1 2350 ATOM C CB LYS A 345 . 26.058 −3.130 2.386 1.00 41.31 . 1 2351 ATOM C CG LYS A 345 . 26.543 −3.512 1.004 1.00 42.99 . 1 2352 ATOM C CD LYS A 345 . 27.828 −4.310 1.096 1.00 44.22 . 1 2353 ATOM C CE LYS A 345 . 28.650 −4.192 −0.168 1.00 45.58 . 1 2354 ATOM N NZ LYS A 345 . 29.192 −2.807 −0.330 1.00 46.93 . 1 2355 ATOM N N LEU A 346 . 23.540 −4.487 3.451 1.00 40.26 . 1 2356 ATOM C CA LEU A 346 . 22.638 −5.625 3.538 1.00 39.90 . 1 2357 ATOM C C LEU A 346 . 21.177 −5.237 3.310 1.00 39.86 . 1 2358 ATOM O O LEU A 346 . 20.446 −5.958 2.639 1.00 38.79 . 1 2359 ATOM C CB LEU A 346 . 22.783 −6.294 4.908 1.00 39.89 . 1 2360 ATOM C CG LEU A 346 . 23.453 −7.671 4.997 1.00 40.15 . 1 2361 ATOM C CD1 LEU A 346 . 24.647 −7.774 4.078 1.00 39.49 . 1 2362 ATOM C CD2 LEU A 346 . 23.866 −7.908 6.447 1.00 40.75 . 1 2363 ATOM N N SER A 347 . 20.754 −4.105 3.870 1.00 40.32 . 1 2364 ATOM C CA SER A 347 . 19.371 −3.665 3.714 1.00 41.45 . 1 2365 ATOM C C SER A 347 . 19.072 −3.275 2.272 1.00 41.71 . 1 2366 ATOM O O SER A 347 . 17.976 −3.515 1.781 1.00 41.34 . 1 2367 ATOM C CB SER A 347 . 19.064 −2.483 4.637 1.00 41.99 . 1 2368 ATOM O OG SER A 347 . 19.846 −1.354 4.306 1.00 44.73 . 1 2369 ATOM N N LYS A 348 . 20.051 −2.681 1.597 1.00 42.55 . 1 2370 ATOM C CA LYS A 348 . 19.876 −2.278 0.204 1.00 43.45 . 1 2371 ATOM C C LYS A 348 . 19.831 −3.504 −0.709 1.00 43.59 . 1 2372 ATOM O O LYS A 348 . 18.919 −3.655 −1.522 1.00 43.47 . 1 2373 ATOM C CB LYS A 348 . 21.013 −1.342 −0.222 1.00 44.46 . 1 2374 ATOM C CG LYS A 348 . 21.030 −0.022 0.542 1.00 45.50 . 1 2375 ATOM C CD LYS A 348 . 22.087 0.947 0.016 1.00 46.51 . 1 2376 ATOM C CE LYS A 348 . 23.498 0.516 0.396 1.00 46.92 . 1 2377 ATOM N NZ LYS A 348 . 24.517 1.446 −0.172 1.00 47.73 . 1 2378 ATOM N N LEU A 349 . 20.812 −4.389 −0.571 1.00 43.34 . 1 2379 ATOM C CA LEU A 349 . 20.847 −5.591 −1.391 1.00 43.52 . 1 2380 ATOM C C LEU A 349 . 19.603 −6.448 −1.209 1.00 43.28 . 1 2381 ATOM O O LEU A 349 . 19.287 −7.285 −2.058 1.00 42.90 . 1 2382 ATOM C CB LEU A 349 . 22.083 −6.423 −1.056 1.00 44.39 . 1 2383 ATOM C CG LEU A 349 . 23.400 −5.951 −1.667 1.00 45.22 . 1 2384 ATOM C CD1 LEU A 349 . 24.573 −6.665 −1.002 1.00 45.46 . 1 2385 ATOM C CD2 LEU A 349 . 23.369 −6.221 −3.163 1.00 45.67 . 1 2386 ATOM N N SER A 350 . 18.895 −6.238 −0.102 1.00 42.92 . 1 2387 ATOM C CA SER A 350 . 17.700 −7.020 0.187 1.00 42.72 . 1 2388 ATOM C C SER A 350 . 16.394 −6.307 −0.171 1.00 42.43 . 1 2389 ATOM O O SER A 350 . 15.314 −6.766 0.197 1.00 42.54 . 1 2390 ATOM C CB SER A 350 . 17.687 −7.434 1.666 1.00 43.13 . 1 2391 ATOM O OG SER A 350 . 17.564 −6.305 2.509 1.00 42.91 . 1 2392 ATOM N N GLY A 351 . 16.491 −5.180 −0.868 1.00 42.33 . 1 2393 ATOM C CA GLY A 351 . 15.290 −4.478 −1.291 1.00 42.47 . 1 2394 ATOM C C GLY A 351 . 14.830 −3.264 −0.512 1.00 42.73 . 1 2395 ATOM O O GLY A 351 . 14.055 −2.456 −1.027 1.00 42.84 . 1 2396 ATOM N N PHE A 352 . 15.290 −3.118 0.724 1.00 42.45 . 1 2397 ATOM C CA PHE A 352 . 14.881 −1.981 1.529 1.00 41.89 . 1 2398 ATOM C C PHE A 352 . 15.382 −0.665 0.957 1.00 42.48 . 1 2399 ATOM O O PHE A 352 . 16.530 −0.546 0.535 1.00 42.89 . 1 2400 ATOM C CB PHE A 352 . 15.336 −2.185 2.972 1.00 40.24 . 1 2401 ATOM C CG PHE A 352 . 14.743 −3.408 3.597 1.00 38.07 . 1 2402 ATOM C CD1 PHE A 352 . 15.306 −4.661 3.369 1.00 38.11 . 1 2403 ATOM C CD2 PHE A 352 . 13.569 −3.324 4.328 1.00 37.44 . 1 2404 ATOM C CE1 PHE A 352 . 14.702 −5.816 3.859 1.00 37.67 . 1 2405 ATOM C CE2 PHE A 352 . 12.956 −4.463 4.821 1.00 37.82 . 1 2406 ATOM C CZ PHE A 352 . 13.524 −5.717 4.586 1.00 38.08 . 1 2407 ATOM N N SER A 353 . 14.495 0.322 0.953 1.00 43.20 . 1 2408 ATOM C CA SER A 353 . 14.779 1.636 0.388 1.00 43.95 . 1 2409 ATOM C C SER A 353 . 15.435 2.640 1.320 1.00 44.18 . 1 2410 ATOM O O SER A 353 . 16.134 3.543 0.862 1.00 44.48 . 1 2411 ATOM C CB SER A 353 . 13.479 2.244 −0.139 1.00 43.87 . 1 2412 ATOM O OG SER A 353 . 12.517 2.316 0.903 1.00 43.66 . 1 2413 ATOM N N LYS A 354 . 15.208 2.495 2.620 1.00 44.16 . 1 2414 ATOM C CA LYS A 354 . 15.773 3.433 3.577 1.00 44.22 . 1 2415 ATOM C C LYS A 354 . 16.399 2.741 4.793 1.00 43.83 . 1 2416 ATOM O O LYS A 354 . 15.824 1.814 5.357 1.00 43.36 . 1 2417 ATOM C CB LYS A 354 . 14.677 4.404 4.026 1.00 45.23 . 1 2418 ATOM C CG LYS A 354 . 15.143 5.521 4.947 1.00 46.81 . 1 2419 ATOM C CD LYS A 354 . 13.962 6.383 5.396 1.00 48.04 . 1 2420 ATOM C CE LYS A 354 . 14.370 7.371 6.488 1.00 49.13 . 1 2421 ATOM N NZ LYS A 354 . 13.185 8.053 7.102 1.00 50.04 . 1 2422 ATOM N N PHE A 355 . 17.583 3.205 5.181 1.00 43.12 . 1 2423 ATOM C CA PHE A 355 . 18.308 2.658 6.322 1.00 42.72 . 1 2424 ATOM C C PHE A 355 . 18.595 3.771 7.321 1.00 42.53 . 1 2425 ATOM O O PHE A 355 . 18.820 4.915 6.930 1.00 42.79 . 1 2426 ATOM C CB PHE A 355 . 19.643 2.058 5.868 1.00 42.19 . 1 2427 ATOM C CG PHE A 355 . 20.587 1.743 7.002 1.00 42.57 . 1 2428 ATOM C CD1 PHE A 355 . 20.523 0.518 7.665 1.00 42.35 . 1 2429 ATOM C CD2 PHE A 355 . 21.526 2.682 7.422 1.00 42.51 . 1 2430 ATOM C CE1 PHE A 355 . 21.384 0.236 8.729 1.00 42.70 . 1 2431 ATOM C CE2 PHE A 355 . 22.392 2.409 8.487 1.00 42.08 . 1 2432 ATOM C CZ PHE A 355 . 22.321 1.186 9.141 1.00 42.53 . 1 2433 ATOM N N GLN A 356 . 18.579 3.438 8.608 1.00 41.93 . 1 2434 ATOM C CA GLN A 356 . 18.893 4.418 9.637 1.00 41.94 . 1 2435 ATOM C C GLN A 356 . 19.065 3.812 11.027 1.00 41.16 . 1 2436 ATOM O O GLN A 356 . 18.340 2.895 11.420 1.00 41.10 . 1 2437 ATOM C CB GLN A 356 . 17.827 5.510 9.700 1.00 43.00 . 1 2438 ATOM C CG GLN A 356 . 16.495 5.058 10.244 1.00 45.37 . 1 2439 ATOM C CD GLN A 356 . 15.672 6.216 10.776 1.00 47.08 . 1 2440 ATOM O OE1 GLN A 356 . 16.117 6.949 11.664 1.00 48.24 . 1 2441 ATOM N NE2 GLN A 356 . 14.465 6.387 10.241 1.00 47.41 . 1 2442 ATOM N N VAL A 357 . 20.044 4.331 11.758 1.00 39.76 . 1 2443 ATOM C CA VAL A 357 . 20.311 3.890 13.119 1.00 39.11 . 1 2444 ATOM C C VAL A 357 . 19.434 4.764 14.002 1.00 38.50 . 1 2445 ATOM O O VAL A 357 . 19.701 5.955 14.145 1.00 38.70 . 1 2446 ATOM C CB VAL A 357 . 21.791 4.114 13.505 1.00 38.85 . 1 2447 ATOM C CG1 VAL A 357 . 21.998 3.836 14.995 1.00 38.41 . 1 2448 ATOM C CG2 VAL A 357 . 22.688 3.220 12.661 1.00 38.06 . 1 2449 ATOM N N ALA A 358 . 18.387 4.178 14.575 1.00 37.50 . 1 2450 ATOM C CA ALA A 358 . 17.463 4.915 15.432 1.00 37.25 . 1 2451 ATOM C C ALA A 358 . 18.084 5.342 16.761 1.00 37.74 . 1 2452 ATOM O O ALA A 358 . 17.823 6.440 17.246 1.00 37.56 . 1 2453 ATOM C CB ALA A 358 . 16.211 4.082 15.689 1.00 36.92 . 1 2454 ATOM N N CYS A 359 . 18.899 4.472 17.349 1.00 37.30 . 1 2455 ATOM C CA CYS A 359 . 19.550 4.774 18.619 1.00 37.19 . 1 2456 ATOM C C CYS A 359 . 20.571 3.696 18.972 1.00 36.35 . 1 2457 ATOM O O CYS A 359 . 20.704 2.695 18.264 1.00 35.29 . 1 2458 ATOM C CB CYS A 359 . 18.509 4.883 19.739 1.00 37.95 . 1 2459 ATOM S SG CYS A 359 . 17.449 3.420 19.929 1.00 41.31 . 1 2460 ATOM N N ARG A 360 . 21.304 3.918 20.057 1.00 35.86 . 1 2461 ATOM C CA ARG A 360 . 22.302 2.959 20.512 1.00 35.27 . 1 2462 ATOM C C ARG A 360 . 22.237 2.838 22.026 1.00 34.42 . 1 2463 ATOM O O ARG A 360 . 22.109 3.843 22.727 1.00 33.80 . 1 2464 ATOM C CB ARG A 360 . 23.718 3.406 20.130 1.00 36.40 . 1 2465 ATOM C CG ARG A 360 . 24.040 3.373 18.650 1.00 38.64 . 1 2466 ATOM C CD ARG A 360 . 25.499 3.766 18.406 1.00 40.13 . 1 2467 ATOM N NE ARG A 360 . 25.832 3.759 16.983 1.00 42.03 . 1 2468 ATOM C CZ ARG A 360 . 27.042 3.503 16.499 1.00 42.16 . 1 2469 ATOM N NH1 ARG A 360 . 28.044 3.230 17.320 1.00 44.19 . 1 2470 ATOM N NH2 ARG A 360 . 27.247 3.507 15.191 1.00 42.74 . 1 2471 ATOM N N ALA A 361 . 22.319 1.606 22.524 1.00 32.81 . 1 2472 ATOM C CA ALA A 361 . 22.316 1.366 23.960 1.00 31.25 . 1 2473 ATOM C C ALA A 361 . 23.762 1.058 24.339 1.00 30.21 . 1 2474 ATOM O O ALA A 361 . 24.495 0.458 23.558 1.00 28.87 . 1 2475 ATOM C CB ALA A 361 . 21.419 0.187 24.304 1.00 31.52 . 1 2476 ATOM N N PHE A 362 . 24.186 1.496 25.519 1.00 30.11 . 1 2477 ATOM C CA PHE A 362 . 25.551 1.228 25.961 1.00 30.13 . 1 2478 ATOM C C PHE A 362 . 26.604 1.726 24.961 1.00 30.49 . 1 2479 ATOM O O PHE A 362 . 27.705 1.173 24.888 1.00 29.86 . 1 2480 ATOM C CB PHE A 362 . 25.722 −0.278 26.163 1.00 29.94 . 1 2481 ATOM C CG PHE A 362 . 24.533 −0.941 26.805 1.00 30.26 . 1 2482 ATOM C CD1 PHE A 362 . 24.029 −2.135 26.297 1.00 30.25 . 1 2483 ATOM C CD2 PHE A 362 . 23.909 −0.371 27.905 1.00 29.86 . 1 2484 ATOM C CE1 PHE A 362 . 22.922 −2.744 26.870 1.00 29.40 . 1 2485 ATOM C CE2 PHE A 362 . 22.801 −0.969 28.490 1.00 29.75 . 1 2486 ATOM C CZ PHE A 362 . 22.303 −2.162 27.969 1.00 30.59 . 1 2487 ATOM N N ASN A 363 . 26.261 2.759 24.192 1.00 30.23 . 1 2488 ATOM C CA ASN A 363 . 27.167 3.333 23.194 1.00 30.08 . 1 2489 ATOM C C ASN A 363 . 27.721 2.286 22.233 1.00 29.87 . 1 2490 ATOM O O ASN A 363 . 28.797 2.472 21.662 1.00 29.09 . 1 2491 ATOM C CB ASN A 363 . 28.350 4.026 23.876 1.00 32.12 . 1 2492 ATOM C CG ASN A 363 . 27.922 5.040 24.918 1.00 34.36 . 1 2493 ATOM O OD1 ASN A 363 . 28.705 5.400 25.802 1.00 36.74 . 1 2494 ATOM N ND2 ASN A 363 . 26.687 5.511 24.821 1.00 34.48 . 1 2495 ATOM N N SER A 364 . 26.996 1.194 22.027 1.00 29.64 . 1 2496 ATOM C CA SER A 364 . 27.518 0.148 21.150 1.00 28.98 . 1 2497 ATOM C C SER A 364 . 26.474 −0.796 20.597 1.00 28.20 . 1 2498 ATOM O O SER A 364 . 26.697 −1.417 19.566 1.00 29.81 . 1 2499 ATOM C CB SER A 364 . 28.573 −0.670 21.897 1.00 29.62 . 1 2500 ATOM O OG SER A 364 . 28.024 −1.235 23.077 1.00 29.81 . 1 2501 ATOM N N LEU A 365 . 25.354 −0.930 21.290 1.00 27.84 . 1 2502 ATOM C CA LEU A 365 . 24.291 −1.809 20.833 1.00 28.48 . 1 2503 ATOM C C LEU A 365 . 23.308 −0.976 20.028 1.00 28.38 . 1 2504 ATOM O O LEU A 365 . 22.534 −0.215 20.591 1.00 28.46 . 1 2505 ATOM C CB LEU A 365 . 23.573 −2.441 22.020 1.00 28.52 . 1 2506 ATOM C CG LEU A 365 . 22.419 −3.377 21.631 1.00 28.94 . 1 2507 ATOM C CD1 LEU A 365 . 22.946 −4.530 20.800 1.00 29.21 . 1 2508 ATOM C CD2 LEU A 365 . 21.733 −3.883 22.862 1.00 30.02 . 1 2509 ATOM N N GLY A 366 . 23.323 −1.129 18.711 1.00 29.20 . 1 2510 ATOM C CA GLY A 366 . 22.426 −0.322 17.905 1.00 29.58 . 1 2511 ATOM C C GLY A 366 . 21.084 −0.922 17.563 1.00 30.46 . 1 2512 ATOM O O GLY A 366 . 20.922 −2.141 17.515 1.00 31.30 . 1 2513 ATOM N N VAL A 367 . 20.108 −0.045 17.354 1.00 30.07 . 1 2514 ATOM C CA VAL A 367 . 18.772 −0.438 16.954 1.00 30.56 . 1 2515 ATOM C C VAL A 367 . 18.634 0.205 15.571 1.00 31.40 . 1 2516 ATOM O O VAL A 367 . 18.447 1.429 15.452 1.00 30.16 . 1 2517 ATOM C CB VAL A 367 . 17.693 0.122 17.910 1.00 30.99 . 1 2518 ATOM C CG1 VAL A 367 . 16.302 −0.295 17.430 1.00 32.20 . 1 2519 ATOM C CG2 VAL A 367 . 17.918 −0.404 19.323 1.00 29.87 . 1 2520 HETA N N MSE A 368 . 18.785 −0.618 14.535 1.00 31.45 . 1 2521 HETA C CA MSE A 368 . 18.704 −0.153 13.153 1.00 31.44 . 1 2522 HETA C C MSE A 368 . 17.336 −0.466 12.534 1.00 32.89 . 1 2523 HETA O O MSE A 368 . 16.701 −1.469 12.880 1.00 32.50 . 1 2524 HETA C CB MSE A 368 . 19.818 −0.806 12.325 1.00 30.32 . 1 2525 HETA C CG MSE A 368 . 21.236 −0.325 12.660 1.00 28.66 . 1 2526 HETA SE SE MSE A 368 . 22.561 −1.404 12.100 1.00 23.72 . 1 2527 HETA C CE MSE A 368 . 22.634 −2.503 13.539 1.00 28.92 . 1 2528 ATOM N N GLU A 369 . 16.883 0.403 11.629 1.00 33.30 . 1 2529 ATOM C CA GLU A 369 . 15.599 0.225 10.965 1.00 34.72 . 1 2530 ATOM C C GLU A 369 . 15.761 0.174 9.444 1.00 35.76 . 1 2531 ATOM O O GLU A 369 . 16.483 0.983 8.850 1.00 35.62 . 1 2532 ATOM C CB GLU A 369 . 14.638 1.366 11.319 1.00 35.16 . 1 2533 ATOM C CG GLU A 369 . 14.399 1.612 12.803 1.00 35.55 . 1 2534 ATOM C CD GLU A 369 . 13.424 2.756 13.038 1.00 36.34 . 1 2535 ATOM O OE1 GLU A 369 . 13.569 3.802 12.369 1.00 38.27 . 1 2536 ATOM O OE2 GLU A 369 . 12.517 2.626 13.888 1.00 36.95 . 1 2537 ATOM N N PHE A 370 . 15.095 −0.794 8.824 1.00 36.72 . 1 2538 ATOM C CA PHE A 370 . 15.134 −0.958 7.375 1.00 37.79 . 1 2539 ATOM C C PHE A 370 . 13.710 −0.716 6.869 1.00 38.43 . 1 2540 ATOM O O PHE A 370 . 12.791 −1.448 7.233 1.00 39.00 . 1 2541 ATOM C CB PHE A 370 . 15.537 −2.391 6.992 1.00 37.58 . 1 2542 ATOM C CG PHE A 370 . 16.916 −2.800 7.430 1.00 37.34 . 1 2543 ATOM C CD1 PHE A 370 . 17.385 −4.082 7.136 1.00 37.84 . 1 2544 ATOM C CD2 PHE A 370 . 17.755 −1.922 8.118 1.00 38.12 . 1 2545 ATOM C CE1 PHE A 370 . 18.663 −4.483 7.516 1.00 37.48 . 1 2546 ATOM C CE2 PHE A 370 . 19.035 −2.311 8.503 1.00 37.13 . 1 2547 ATOM C CZ PHE A 370 . 19.493 −3.590 8.203 1.00 38.01 . 1 2548 ATOM N N TYR A 371 . 13.513 0.305 6.044 1.00 39.56 . 1 2549 ATOM C CA TYR A 371 . 12.177 0.570 5.511 1.00 40.76 . 1 2550 ATOM C C TYR A 371 . 12.052 0.005 4.104 1.00 41.42 . 1 2551 ATOM O O TYR A 371 . 12.958 0.165 3.287 1.00 41.33 . 1 2552 ATOM C CB TYR A 371 . 11.887 2.073 5.488 1.00 40.57 . 1 2553 ATOM C CG TYR A 371 . 11.826 2.694 6.858 1.00 39.93 . 1 2554 ATOM C CD1 TYR A 371 . 12.985 3.102 7.513 1.00 40.18 . 1 2555 ATOM C CD2 TYR A 371 . 10.611 2.835 7.523 1.00 39.94 . 1 2556 ATOM C CE1 TYR A 371 . 12.938 3.638 8.796 1.00 39.69 . 1 2557 ATOM C CE2 TYR A 371 . 10.552 3.367 8.810 1.00 40.30 . 1 2558 ATOM C CZ TYR A 371 . 11.721 3.766 9.438 1.00 40.22 . 1 2559 ATOM O OH TYR A 371 . 11.670 4.300 10.707 1.00 41.01 . 1 2560 ATOM N N LYS A 372 . 10.933 −0.661 3.825 1.00 42.58 . 1 2561 ATOM C CA LYS A 372 . 10.705 −1.241 2.502 1.00 43.82 . 1 2562 ATOM C C LYS A 372 . 11.040 −0.256 1.391 1.00 44.18 . 1 2563 ATOM O O LYS A 372 . 11.922 −0.578 0.567 1.00 38.85 . 1 2564 ATOM C CB LYS A 372 . 9.253 −1.680 2.339 1.00 43.85 . 1 2565 ATOM C CG LYS A 372 . 8.873 −2.877 3.161 1.00 44.46 . 1 2566 ATOM C CD LYS A 372 . 7.548 −3.440 2.696 1.00 44.97 . 1 2567 ATOM C CE LYS A 372 . 7.664 −4.044 1.307 1.00 44.91 . 1 2568 ATOM N NZ LYS A 372 . 6.409 −4.735 0.929 1.00 44.78 . 1 2569 ATOM O OXT LYS A 372 . 10.417 0.826 1.356 1.00 38.85 . 1 2570 #372 . TER # . . LYS A 372 . . . . . . . 1 2571 HETA N N SAM . 1699 . 17.294 −13.891 21.866 1.00 55.09 . 2 2572 HETA C CA SAM . 1699 . 18.274 −14.810 21.161 1.00 54.84 . 2 2573 HETA C C SAM . 1699 . 19.536 −14.875 22.110 1.00 55.61 . 2 2574 HETA O O SAM . 1699 . 20.383 −13.914 22.050 1.00 56.23 . 2 2575 HETA O OXT SAM . 1699 . 19.642 −15.874 22.876 1.00 56.31 . 2 2576 HETA C CB SAM . 1699 . 18.593 −14.320 19.751 1.00 53.22 . 2 2577 HETA C CG SAM . 1699 . 19.546 −14.998 18.748 1.00 50.51 . 2 2578 HETA S SD SAM . 1699 . 19.218 −16.792 18.565 1.00 48.48 . 2 2579 HETA C CE SAM . 1699 . 20.785 −17.521 18.105 1.00 49.32 . 2 2580 HETA C C5* SAM . 1699 . 18.053 −16.711 17.194 1.00 46.63 . 2 2581 HETA C C4* SAM . 1699 . 17.412 −17.996 16.710 1.00 43.35 . 2 2582 HETA O O4* SAM . 1699 . 17.155 −18.039 15.282 1.00 41.46 . 2 2583 HETA C C3* SAM . 1699 . 18.121 −19.341 16.925 1.00 41.90 . 2 2584 HETA O O3* SAM . 1699 . 18.156 −19.579 18.313 1.00 41.29 . 2 2585 HETA C C2* SAM . 1699 . 17.186 −20.321 16.150 1.00 40.79 . 2 2586 HETA O O2* SAM . 1699 . 16.423 −21.288 16.748 1.00 40.17 . 2 2587 HETA C C1* SAM . 1699 . 16.542 −19.368 15.157 1.00 40.06 . 2 2588 HETA N N9 SAM . 1699 . 16.661 −19.751 13.747 1.00 39.27 . 2 2589 HETA C C8 SAM . 1699 . 17.816 −20.242 13.166 1.00 38.71 . 2 2590 HETA N N7 SAM . 1699 . 17.628 −20.520 11.932 1.00 38.99 . 2 2591 HETA C C5 SAM . 1699 . 16.297 −20.207 11.683 1.00 38.12 . 2 2592 HETA C C6 SAM . 1699 . 15.502 −20.321 10.460 1.00 38.03 . 2 2593 HETA N N6 SAM . 1699 . 16.021 −20.791 9.344 1.00 37.16 . 2 2594 HETA N N1 SAM . 1699 . 14.231 −19.914 10.601 1.00 37.89 . 2 2595 HETA C C2 SAM . 1699 . 13.678 −19.428 11.750 1.00 38.37 . 2 2596 HETA N N3 SAM . 1699 . 14.370 −19.314 12.887 1.00 37.89 . 2 2597 HETA C C4 SAM . 1699 . 15.659 −19.716 12.780 1.00 38.33 . 2 2598 HETA O O HOH . 1 . 25.448 −24.975 24.794 1.00 47.52 . 3 2599 HETA O O HOH . 2 . 30.351 1.326 11.992 1.00 30.85 . 3 2600 HETA O O HOH . 3 . 10.954 −13.110 20.940 1.00 36.87 . 3 2601 HETA O O HOH . 4 . 26.806 −18.729 7.490 1.00 43.15 . 3 2602 HETA O O HOH . 5 . 55.037 −12.443 19.756 1.00 24.68 . 3 2603 HETA O O HOH . 6 . 21.237 −19.716 14.660 1.00 36.01 . 3 2604 HETA O O HOH . 7 . 55.277 −12.339 16.930 1.00 24.55 . 3 2605 HETA O O HOH . 8 . 0.551 −0.284 22.475 1.00 45.51 . 3 2606 HETA O O HOH . 9 . 20.057 −9.348 13.720 1.00 32.68 . 3 2607 HETA O O HOH . 10 . 27.245 −6.601 14.459 1.00 29.25 . 3 2608 HETA O O HOH . 11 . 13.897 −11.630 20.148 1.00 39.64 . 3 2609 HETA O O HOH . 12 . 62.861 −8.145 14.289 1.00 48.33 . 3 2610 HETA O O HOH . 13 . 44.830 −18.540 22.115 1.00 31.79 . 3 2611 HETA O O HOH . 14 . −1.081 −7.140 24.008 1.00 41.96 . 3 2612 HETA O O HOH . 15 . 62.274 −0.268 28.598 1.00 36.93 . 3 2613 HETA O O HOH . 16 . 18.955 −11.921 35.209 1.00 47.27 . 3 2614 HETA O O HOH . 17 . 19.779 −9.943 33.802 1.00 41.87 . 3 2615 HETA O O HOH . 18 . 55.501 −1.392 13.069 1.00 34.71 . 3 2616 HETA O O HOH . 19 . 12.816 −9.086 19.859 1.00 36.25 . 3 2617 HETA O O HOH . 20 . 32.672 −0.873 6.833 1.00 38.83 . 3 2618 HETA O O HOH . 21 . 36.840 −2.468 16.359 1.00 32.58 . 3 2619 HETA O O HOH . 22 . 35.782 4.571 26.112 1.00 43.99 . 3 2620 HETA O O HOH . 23 . 32.376 4.596 24.870 1.00 46.14 . 3 2621 HETA O O HOH . 24 . 26.828 7.385 27.041 1.00 37.91 . 3 2622 HETA O O HOH . 25 . 12.746 −0.997 30.081 1.00 42.24 . 3 2623 HETA O O HOH . 26 . 21.581 −8.228 20.253 1.00 51.29 . 3 2624 HETA O O HOH . 27 . 68.633 −11.604 22.653 1.00 47.67 . 3 2625 HETA O O HOH . 28 . 43.730 −0.762 27.131 1.00 52.33 . 3 2626 HETA O O HOH . 29 . 52.011 −17.751 23.019 1.00 41.64 . 3 2627 HETA O O HOH . 30 . −3.837 −10.738 23.791 1.00 58.53 . 3 2628 HETA O O HOH . 31 . 14.646 −11.703 16.769 1.00 35.27 . 3 2629 HETA O O HOH . 32 . 3.648 −19.692 30.136 1.00 39.07 . 3 2630 HETA O O HOH . 33 . 26.455 −9.043 11.616 1.00 40.05 . 3 2631 HETA O O HOH . 34 . 29.894 11.349 37.467 1.00 47.80 . 3 2632 HETA O O HOH . 35 . 22.899 8.278 33.361 1.00 43.79 . 3 2633 HETA O O HOH . 36 . 40.741 −8.327 5.057 1.00 53.92 . 3 2634 HETA O O HOH . 37 . 9.439 −6.419 32.797 1.00 56.42 . 3 2635 HETA O O HOH . 38 . 32.193 4.145 13.342 1.00 48.29 . 3 2636 HETA O O HOH . 39 . 11.056 −18.368 −0.605 1.00 50.23 . 3 2637 HETA O O HOH . 40 . 18.124 −23.147 17.707 1.00 39.38 . 3 2638 HETA O O HOH . 41 . 12.644 5.548 15.129 1.00 54.07 . 3 2639 HETA O O HOH . 42 . 29.377 2.089 19.246 1.00 43.57 . 3 2640 HETA O O HOH . 43 . 18.530 −19.173 26.434 1.00 43.59 . 3 2641 HETA O O HOH . 44 . 37.364 −7.564 15.404 1.00 35.46 . 3 2642 HETA O O HOH . 45 . 25.541 −8.022 17.856 1.00 30.55 . 3 2643 HETA O O HOH . 46 . 48.976 4.613 −0.967 1.00 48.39 . 3 2644 HETA O O HOH . 47 . 22.979 6.277 29.829 1.00 48.53 . 3 2645 HETA O O HOH . 48 . 53.479 4.385 16.916 1.00 54.23 . 3 2646 HETA O O HOH . 49 . 19.785 −17.290 13.462 1.00 33.95 . 3 2647 HETA O O HOH . 50 . 15.620 −13.333 19.023 1.00 40.32 . 3 2648 HETA O O HOH . 51 . 27.901 −23.843 15.310 1.00 54.62 . 3 2649 HETA O O HOH . 52 . 68.322 −10.139 18.576 1.00 52.59 . 3 2650 HETA O O HOH . 53 . 14.401 −6.752 31.193 1.00 53.75 . 3 2651 HETA O O HOH . 54 . 22.798 −15.322 18.391 1.00 39.77 . 3 2652 HETA O O HOH . 55 . 43.534 3.847 −10.966 1.00 40.04 . 3 2653 HETA O O HOH . 56 . 40.260 −2.461 4.990 1.00 38.24 . 3 2654 HETA O O HOH . 57 . 9.829 −11.496 29.334 1.00 41.39 . 3 2655 HETA O O HOH . 58 . 28.322 −14.552 1.353 1.00 49.36 . 3 2656 HETA O O HOH . 59 . 29.774 4.265 8.944 1.00 55.13 . 3 2657 HETA O O HOH . 60 . 64.402 −12.137 22.772 1.00 39.56 . 3 2658 HETA O O HOH . 61 . 37.116 4.890 −10.735 1.00 54.29 . 3 2659 HETA O O HOH . 62 . −2.278 −13.973 20.757 1.00 45.88 . 3 2660 HETA O O HOH . 63 . 53.097 2.157 14.247 1.00 40.34 . 3 2661 HETA O O HOH . 64 . 58.984 −14.238 −0.932 1.00 54.97 . 3 2662 HETA O O HOH . 65 . 32.451 3.125 29.166 1.00 33.50 . 3 2663 HETA O O HOH . 66 . 65.043 −8.862 22.979 1.00 55.37 . 3 2664 HETA O O HOH . 67 . 13.814 −12.478 30.979 1.00 49.66 . 3 2665 HETA O O HOH . 68 . 19.551 −18.752 22.150 1.00 55.23 . 3 2666 HETA O O HOH . 69 . 40.106 −16.757 −3.566 1.00 59.91 . 3 2667 HETA O O HOH . 70 . 59.489 −18.694 15.599 1.00 63.41 . 3 2668 HETA O O HOH . 71 . 39.652 −5.749 29.163 1.00 49.72 . 3 2669 HETA O O HOH . 72 . 48.484 8.637 8.908 1.00 53.79 . 3 2670 HETA O O HOH . 73 . 15.032 −30.469 25.858 1.00 53.07 . 3 2671 HETA O O HOH . 74 . 30.940 5.764 11.825 1.00 46.71 . 3 2672 HETA O O HOH . 75 . 31.069 4.725 35.518 1.00 43.07 . 3 2673 HETA O O HOH . 76 . 39.606 −12.569 3.470 1.00 44.05 . 3 2674 HETA O O HOH . 77 . 12.576 −5.104 31.760 1.00 56.51 . 3 2675 HETA O O HOH . 78 . 53.229 4.741 14.394 1.00 46.72 . 3 2676 HETA O O HOH . 79 . 5.865 −11.888 −6.782 1.00 55.09 . 3 2677 HETA O O HOH . 80 . 58.039 5.864 14.090 1.00 56.59 . 3 2678 HETA O O HOH . 81 . 17.082 −20.744 20.526 1.00 63.39 . 3 2679 HETA O O HOH . 82 . 19.843 −31.476 30.092 1.00 64.95 . 3 2680 HETA O O HOH . 83 . 26.972 −15.699 22.080 1.00 57.20 . 3 2681 HETA O O HOH . 84 . 13.322 −7.664 −1.797 1.00 48.98 . 3 2682 HETA O O HOH . 85 . 25.174 −29.912 28.382 1.00 46.01 . 3 2683 HETA O O HOH . 86 . 29.944 8.591 30.585 1.00 47.91 . 3 2684 HETA O O HOH . 87 . 28.595 −7.947 5.498 1.00 49.68 . 3 2685 HETA O O HOH . 88 . 37.765 0.800 −1.136 1.00 51.23 . 3 2686 HETA O O HOH . 89 . 45.336 −30.578 40.736 1.00 58.30 . 3 2687 HETA O O HOH . 90 . 37.550 5.021 14.777 1.00 46.35 . 3 2688 HETA O O HOH . 91 . 21.502 −14.305 −1.101 1.00 39.72 . 3 2689 HETA O O HOH . 92 . 35.083 −13.175 30.519 1.00 31.79 . 3 2690 HETA O O HOH . 93 . 12.914 −3.911 −3.830 1.00 47.06 . 3 2691 HETA O O HOH . 94 . 66.973 −8.343 26.009 1.00 58.37 . 3 2692 HETA O O HOH . 95 . 3.281 −23.452 14.643 1.00 61.26 . 3 2693 HETA O O HOH . 96 . 50.019 −14.502 −0.511 1.00 61.19 . 3 2694 HETA O O HOH . 97 . −7.849 −7.471 16.034 1.00 60.48 . 3 2695 HETA O O HOH . 98 . 50.870 6.817 15.878 1.00 65.06 . 3 2696 HETA O O HOH . 99 . 14.744 −17.831 24.245 1.00 60.82 . 3 2697 HETA O O HOH . 100 . 2.645 −22.418 23.808 1.00 48.87 . 3 2698 HETA O O HOH . 101 . 33.892 −9.076 11.587 1.00 42.26 . 3 2699 HETA O O HOH . 102 . 0.236 −17.410 11.528 1.00 54.56 . 3 2700 HETA O O HOH . 103 . 10.671 −25.295 5.237 1.00 59.27 . 3 2701 HETA O O HOH . 104 . 9.175 −26.518 8.798 1.00 49.10 . 3 2702 HETA O O HOH . 105 . 9.966 −29.726 10.464 1.00 60.81 . 3 2703 HETA O O HOH . 106 . 57.436 −9.546 −1.613 1.00 50.67 . 3 2704 HETA O O HOH . 107 . 9.492 −8.085 −2.181 1.00 59.61 . 3 2705 HETA O O HOH . 108 . 11.792 −3.592 29.812 1.00 49.30 . 3 2706 HETA O O HOH . 109 . 4.420 −18.264 7.800 1.00 52.32 . 3 2707 HETA O O HOH . 110 . 10.126 7.491 7.707 1.00 56.10 . 3 2708 HETA O O HOH . 111 . 47.845 −12.746 1.095 1.00 51.05 . 3 2709 HETA O O HOH . 112 . 1.136 3.912 10.693 1.00 59.52 . 3 2710 HETA O O HOH . 113 . 19.887 8.304 23.558 1.00 64.36 . 3 2711 HETA O O HOH . 114 . −7.040 0.156 24.015 1.00 56.37 . 3 2712 HETA O O HOH . 115 . 21.172 9.673 26.412 1.00 55.74 . 3 2713 HETA O O HOH . 116 . 4.299 −14.395 4.697 1.00 40.30 . 3 2714 HETA O O HOH . 117 . 47.934 −4.195 26.754 1.00 73.82 . 3 2715 HETA O O HOH . 118 . 33.616 −17.295 7.191 1.00 63.41 . 3 2716 HETA O O HOH . 119 . 48.261 −29.698 36.402 1.00 53.99 . 3 2717 HETA O O HOH . 120 . 58.239 −12.518 7.860 1.00 53.67 . 3 2718 HETA O O HOH . 121 . 56.307 −5.216 3.845 1.00 44.37 . 3 2719 HETA O O HOH . 122 . 10.763 −17.665 32.455 1.00 53.87 . 3 2720 HETA O O HOH . 124 . 12.621 −0.546 32.635 1.00 48.35 . 3 2721 HETA O O HOH . 125 . 6.246 −29.604 15.795 1.00 54.87 . 3 2722 HETA O O HOH . 126 . 35.831 1.049 2.622 1.00 62.85 . 3 2723 HETA O O HOH . 127 . 21.568 −11.638 22.525 1.00 57.98 . 3 2724 HETA O O HOH . 128 . 39.267 3.328 −9.929 1.00 54.10 . 3 2725 HETA O O HOH . 129 . 43.337 0.785 24.516 1.00 53.35 . 3 2726 HETA O O HOH . 130 . 51.603 −31.679 34.180 1.00 50.19 . 3 2727 HETA O O HOH . 131 . −4.730 −6.065 20.152 1.00 57.62 . 3 2728 HETA O O HOH . 132 . 56.965 −18.365 17.898 1.00 55.06 . 3 2729 HETA O O HOH . 133 . 19.152 5.981 4.260 1.00 52.11 . 3 2730 HETA O O HOH . 134 . 28.580 −26.048 20.675 1.00 56.96 . 3 2731 HETA O O HOH . 135 . 40.763 4.576 14.342 1.00 50.93 . 3 2732 HETA O O HOH . 136 . 34.005 3.413 18.275 1.00 53.08 . 3 2733 HETA O O HOH . 137 . 0.002 −20.521 11.733 1.00 63.38 . 3 2734 HETA O O HOH . 138 . −4.108 −3.997 15.513 1.00 62.32 . 3 2735 HETA O O HOH . 139 . 32.475 −21.977 4.032 1.00 47.02 . 3 2736 HETA O O HOH . 140 . 50.923 −11.919 −2.990 1.00 61.02 . 3 2737 HETA O O HOH . 141 . 38.319 −33.085 31.693 1.00 62.30 . 3 2738 HETA O O HOH . 142 . 25.741 −18.841 33.082 1.00 40.72 . 3 2739 HETA O O HOH . 143 . 3.408 −10.188 1.717 1.00 46.45 . 3 2740 HETA O O HOH . 144 . 2.793 6.194 1.546 1.00 58.08 . 3 2741 HETA O O HOH . 145 . 18.222 −16.026 34.337 1.00 50.43 . 3 2742 HETA O O HOH . 146 . 16.251 −14.986 38.115 1.00 50.49 . 3 2743 HETA O O HOH . 147 . 3.975 0.393 11.458 1.00 48.81 . 3 2744 HETA O O HOH . 148 . 29.304 10.973 33.910 1.00 48.07 . 3 2745 HETA O O HOH . 149 . 0.733 0.192 18.763 1.00 46.87 . 3 2746 HETA O O HOH . 150 . 27.518 −7.442 1.334 1.00 47.24 . 3 2747 HETA O O HOH . 151 . 66.895 −1.306 8.013 1.00 58.30 . 3 2748 HETA O O HOH . 152 . 51.237 −28.628 8.876 1.00 51.57 . 3 2749 HETA O O HOH . 153 . 21.170 6.625 21.692 1.00 50.05 . 3 2750 HETA O O HOH . 154 . 22.444 7.167 18.001 1.00 50.67 . 3 2751 HETA O O HOH . 155 . 19.534 2.475 2.077 1.00 50.31 . 3 2752 HETA O O HOH . 156 . 14.137 10.195 5.057 1.00 58.41 . 3 2753 HETA O O HOH . 157 . 53.114 −24.864 4.763 1.00 59.80 . 3 2754 HETA O O HOH . 158 . 0.428 −8.838 27.224 1.00 60.86 . 3 2755 HETA O O HOH . 159 . 51.023 −21.690 25.651 1.00 40.27 . 3 2756 HETA O O HOH . 160 . 32.073 6.012 8.257 1.00 52.62 . 3 2757 HETA O O HOH . 161 . 49.327 −24.485 21.771 1.00 61.29 . 3 2758 HETA O O HOH . 162 . 26.731 0.828 3.031 1.00 41.47 . 3 2759 HETA O O HOH . 163 . 0.459 3.761 13.860 1.00 61.29 . 3 2760 HETA O O HOH . 164 . −0.633 −11.972 18.662 1.00 37.60 . 3 2761 HETA O O HOH . 165 . 2.345 −22.939 18.043 1.00 46.31 . 3 2762 HETA O O HOH . 166 . 22.341 8.853 30.760 1.00 60.69 . 3 2763 HETA O O HOH . 167 . 6.468 −18.576 −2.786 1.00 54.43 . 3 2764 HETA O O HOH . 168 . 35.480 −3.844 9.047 1.00 52.31 . 3 2765 HETA O O HOH . 169 . 0.047 −6.851 8.186 1.00 46.56 . 3 2766 HETA O O HOH . 170 . 44.630 −16.869 −1.354 1.00 56.53 . 3 2767 HETA O O HOH . 171 . 57.414 1.648 18.115 1.00 57.76 . 3 2768 HETA O O HOH . 172 . 65.019 3.285 6.058 1.00 55.24 . 3 2769 HETA O O HOH . 173 . 22.117 6.159 5.659 1.00 62.41 . 3 2770 HETA O O HOH . 174 . 9.576 −33.403 19.285 1.00 55.81 . 3 2771 HETA O O HOH . 175 . 27.022 −21.653 −2.698 1.00 50.96 . 3 2772 HETA O O HOH . 176 . 37.147 −6.655 10.897 1.00 53.84 . 3 2773 HETA O O HOH . 177 . 39.917 0.662 −11.855 1.00 55.28 . 3 2774 HETA O O HOH . 178 . 58.116 −1.488 14.706 1.00 54.14 . 3 2775 HETA O O HOH . 179 . 30.407 −13.381 −2.502 1.00 63.07 . 3 2776 HETA O O HOH . 180 . 49.055 5.821 22.836 1.00 48.89 . 3 2777 HETA O O HOH . 181 . 20.350 −8.870 −3.980 1.00 49.76 . 3 2778 HETA O O HOH . 182 . 8.317 −21.721 1.387 1.00 46.98 . 3 2779 HETA O O HOH . 183 . 7.740 −12.326 32.303 1.00 59.01 . 3 2780 HETA O O HOH . 184 . −1.603 1.876 15.261 1.00 54.08 . 3 2781 HETA O O HOH . 185 . 51.710 −28.010 25.609 1.00 61.62 . 3 2782 HETA O O HOH . 186 . 56.322 6.932 19.411 1.00 56.95 . 3 2783 HETA O O HOH . 187 . 19.919 −35.532 25.413 1.00 53.84 . 3 2784 HETA O O HOH . 188 . 24.044 4.516 24.384 1.00 37.64 . 3 2785 HETA O O HOH . 189 . 33.459 6.658 22.589 1.00 57.92 . 3 2786 HETA O O HOH . 190 . −1.938 −8.878 4.792 1.00 56.16 . 3 2787 HETA O O HOH . 191 . 3.677 −18.162 1.237 1.00 59.68 . 3 2788 HETA O O HOH . 192 . 63.026 0.227 20.597 1.00 46.19 . 3 2789 HETA O O HOH . 193 . 33.355 7.153 29.621 1.00 53.28 . 3 2790 HETA O O HOH . 194 . 34.540 −20.574 6.274 1.00 56.02 . 3 2791 HETA O O HOH . 195 . 48.841 3.028 25.401 1.00 54.92 . 3 2792 HETA O O HOH . 196 . 32.612 −1.728 4.400 1.00 52.31 . 3 2793 HETA O O HOH . 197 . 39.719 −30.922 46.727 1.00 56.93 . 3 2794 HETA O O HOH . 198 . 19.174 −22.742 35.061 1.00 61.75 . 3 2795 HETA O O HOH . 199 . 29.939 13.240 34.818 1.00 52.41 . 3 2796 HETA O O HOH . 200 . −5.656 −15.179 16.252 1.00 66.80 . 3 2797 HETA O O HOH . 201 . 59.158 −14.284 3.282 1.00 57.88 . 3 2798 HETA O O HOH . 202 . 37.039 5.737 7.801 1.00 56.19 . 3 2799 HETA O O HOH . 203 . 31.777 −8.388 −1.302 1.00 53.39 . 3 2800 HETA O O HOH . 204 . −3.065 −8.434 21.822 1.00 62.20 . 3 2801 HETA O O HOH . 205 . 27.391 −30.285 30.168 1.00 54.00 . 3 2802 HETA O O HOH . 206 . −1.652 −10.292 13.774 1.00 45.64 . 3 2803 HETA O O HOH . 207 . 41.199 3.267 −11.258 1.00 54.41 . 3 2804 HETA O O HOH . 208 . 10.084 −15.669 −0.644 1.00 60.70 . 3 2805 HETA O O HOH . 209 . 8.032 −35.641 19.676 1.00 55.48 . 3 2806 HETA O O HOH . 210 . 26.870 −11.619 −4.358 1.00 51.60 . 3 2807 HETA O O HOH . 211 . 21.399 9.551 18.948 1.00 56.53 . 3 2808 HETA O O HOH . 212 . 41.822 −7.113 −2.949 1.00 58.10 . 3 2809 HETA O O HOH . 213 . 18.159 10.978 15.317 1.00 52.43 . 3 2810 HETA O O HOH . 214 . 26.274 −30.981 35.189 1.00 57.40 . 3 2811 HETA O O HOH . 215 . 18.795 −24.058 30.847 1.00 65.89 . 3 2812 HETA O O HOH . 216 . 64.520 −3.455 18.625 1.00 51.48 . 3 2813 HETA O O HOH . 217 . 11.371 −20.563 28.173 1.00 59.82 . 3 2814 HETA O O HOH . 218 . 57.158 −9.447 7.492 1.00 40.05 . 3 2815 HETA O O HOH . 219 . −8.824 −9.760 14.936 1.00 58.42 . 3 2816 HETA O O HOH . 220 . 29.763 −13.013 3.292 1.00 49.47 . 3 2817 HETA O O HOH . 221 . 8.054 −22.792 5.504 1.00 46.75 . 3 2818 HETA O O HOH . 222 . 41.745 −13.075 0.280 1.00 59.28 . 3 2819 HETA O O HOH . 223 . 7.417 5.713 26.370 1.00 64.71 . 3 2820 HETA O O HOH . 224 . 23.657 −12.725 −2.446 1.00 62.14 . 3 2821 HETA O O HOH . 225 . 32.648 −3.312 −0.086 1.00 60.77 . 3 2822 HETA O O HOH . 226 . 36.261 −13.778 8.443 1.00 43.82 . 3 2823 HETA O O HOH . 227 . 37.815 −7.358 25.762 1.00 56.21 . 3 2824 HETA O O HOH . 228 . 65.410 0.202 4.637 1.00 65.20 . 3 2825 HETA O O HOH . 229 . −3.642 −13.304 25.041 1.00 62.25 . 3 2826 HETA O O HOH . 230 . 12.440 −29.415 26.761 1.00 57.32 . 3 2827 HETA O O HOH . 231 . 11.548 3.857 30.827 1.00 44.69 . 3 2828 HETA O O HOH . 232 . 58.640 −14.174 10.440 1.00 63.60 . 3 2829 HETA O O HOH . 233 . 23.314 −5.945 −6.495 1.00 47.87 . 3 2830 HETA O O HOH . 234 . 66.257 −9.941 7.383 1.00 62.96 . 3 2831 HETA O O HOH . 235 . −6.899 −11.844 18.949 1.00 62.18 . 3 2832 HETA O O HOH . 236 . 53.449 −8.068 −1.473 1.00 46.54 . 3 2833 HETA O O HOH . 237 . 14.861 7.497 28.722 1.00 55.08 . 3 2834

APPENDIX B ATOM TYPE RES # X Y Z OCC B ATOM ATOM N N ARG A 8 . −17.645 −8.040 54.497 1.00 49.11 . 1 1 ATOM C CA ARG A 8 . −16.423 −8.635 55.109 1.00 49.22 . 1 2 ATOM C C ARG A 8 . −16.371 −10.173 54.976 1.00 49.53 . 1 3 ATOM O O ARG A 8 . −17.231 −10.917 55.488 1.00 49.73 . 1 4 ATOM C CB ARG A 8 . −16.316 −8.213 56.567 1.00 49.11 . 1 5 ATOM C CG ARG A 8 . −14.880 −8.258 57.055 1.00 50.14 . 1 6 ATOM C CD ARG A 8 . −13.973 −7.598 56.031 1.00 48.73 . 1 7 ATOM N NE ARG A 8 . −12.587 −8.038 56.190 1.00 49.18 . 1 8 ATOM C CZ ARG A 8 . −11.565 −7.595 55.456 1.00 48.58 . 1 9 ATOM N NH1 ARG A 8 . −11.762 −6.691 54.498 1.00 48.76 . 1 10 ATOM N NH2 ARG A 8 . −10.339 −8.046 55.687 1.00 47.39 . 1 11 ATOM N N LYS A 9 . −15.335 −10.630 54.276 1.00 48.40 . 1 12 ATOM C CA LYS A 9 . −15.122 −12.032 53.969 1.00 47.03 . 1 13 ATOM C C LYS A 9 . −13.664 −12.384 54.324 1.00 46.69 . 1 14 ATOM O O LYS A 9 . −13.034 −11.676 55.112 1.00 45.75 . 1 15 ATOM C CB LYS A 9 . −15.385 −12.204 52.462 1.00 47.09 . 1 16 ATOM C CG LYS A 9 . −16.592 −11.393 51.948 1.00 46.84 . 1 17 ATOM C CD LYS A 9 . −17.307 −12.080 50.796 1.00 47.04 . 1 18 ATOM C CE LYS A 9 . −18.619 −11.378 50.456 1.00 47.42 . 1 19 ATOM N NZ LYS A 9 . −19.483 −12.194 49.543 1.00 47.57 . 1 20 ATOM N N PRO A 10 . −13.124 −13.500 53.780 1.00 46.44 . 1 21 ATOM C CA PRO A 10 . −11.728 −13.907 54.049 1.00 46.41 . 1 22 ATOM C C PRO A 10 . −10.778 −13.231 53.051 1.00 46.31 . 1 23 ATOM O O PRO A 10 . −11.156 −12.249 52.441 1.00 45.87 . 1 24 ATOM C CB PRO A 10 . −11.769 −15.419 53.838 1.00 46.56 . 1 25 ATOM C CG PRO A 10 . −12.775 −15.562 52.760 1.00 46.36 . 1 26 ATOM C CD PRO A 10 . −13.877 −14.639 53.217 1.00 46.95 . 1 27 ATOM N N SER A 11 . −9.568 −13.764 52.859 1.00 47.00 . 1 28 ATOM C CA SER A 11 . −8.623 −13.181 51.899 1.00 46.33 . 1 29 ATOM C C SER A 11 . −9.122 −13.216 50.431 1.00 45.46 . 1 30 ATOM O O SER A 11 . −8.349 −13.297 49.464 1.00 45.49 . 1 31 ATOM C CB SER A 11 . −7.270 −13.870 51.983 1.00 48.29 . 1 32 ATOM O OG SER A 11 . −6.442 −13.441 50.911 1.00 51.18 . 1 33 ATOM N N GLU A 12 . −10.430 −13.186 50.265 1.00 43.64 . 1 34 ATOM C CA GLU A 12 . −10.983 −13.114 48.941 1.00 42.03 . 1 35 ATOM C C GLU A 12 . −11.165 −11.594 48.744 1.00 39.82 . 1 36 ATOM O O GLU A 12 . −11.655 −11.118 47.707 1.00 39.12 . 1 37 ATOM C CB GLU A 12 . −12.304 −13.855 48.855 1.00 44.42 . 1 38 ATOM C CG GLU A 12 . −13.153 −13.775 50.062 1.00 47.37 . 1 39 ATOM C CD GLU A 12 . −14.553 −14.302 49.784 1.00 49.67 . 1 40 ATOM O OE1 GLU A 12 . −15.252 −14.693 50.752 1.00 50.16 . 1 41 ATOM O OE2 GLU A 12 . −14.952 −14.309 48.587 1.00 50.81 . 1 42 ATOM N N ILE A 13 . −10.784 −10.851 49.782 1.00 36.79 . 1 43 ATOM C CA ILE A 13 . −10.827 −9.399 49.757 1.00 34.12 . 1 44 ATOM C C ILE A 13 . −9.656 −8.958 48.846 1.00 33.48 . 1 45 ATOM O O ILE A 13 . −9.801 −8.039 48.051 1.00 31.42 . 1 46 ATOM C CB ILE A 13 . −10.651 −8.835 51.186 1.00 34.25 . 1 47 ATOM C CG1 ILE A 13 . −11.972 −8.960 51.946 1.00 34.33 . 1 48 ATOM C CG2 ILE A 13 . −10.150 −7.414 51.141 1.00 33.38 . 1 49 ATOM C CD1 ILE A 13 . −13.065 −8.058 51.387 1.00 34.85 . 1 50 ATOM N N PHE A 14 . −8.515 −9.642 48.961 1.00 32.68 . 1 51 ATOM C CA PHE A 14 . −7.334 −9.330 48.132 1.00 32.11 . 1 52 ATOM C C PHE A 14 . −7.694 −9.541 46.637 1.00 32.27 . 1 53 ATOM O O PHE A 14 . −7.322 −8.733 45.772 1.00 30.49 . 1 54 ATOM C CB PHE A 14 . −6.154 −10.245 48.572 1.00 32.88 . 1 55 ATOM C CG PHE A 14 . −4.805 −9.935 47.913 1.00 32.73 . 1 56 ATOM C CD1 PHE A 14 . −4.532 −8.683 47.360 1.00 32.87 . 1 57 ATOM C CD2 PHE A 14 . −3.798 −10.895 47.901 1.00 33.29 . 1 58 ATOM C CE1 PHE A 14 . −3.281 −8.384 46.805 1.00 32.88 . 1 59 ATOM C CE2 PHE A 14 . −2.526 −10.592 47.333 1.00 33.29 . 1 60 ATOM C CZ PHE A 14 . −2.294 −9.320 46.788 1.00 31.60 . 1 61 ATOM N N LYS A 15 . −8.427 −10.614 46.335 1.00 30.59 . 1 62 ATOM C CA LYS A 15 . −8.822 −10.870 44.947 1.00 31.49 . 1 63 ATOM C C LYS A 15 . −9.754 −9.762 44.414 1.00 30.20 . 1 64 ATOM O O LYS A 15 . −9.630 −9.329 43.258 1.00 28.67 . 1 65 ATOM C CB LYS A 15 . −9.498 −12.249 44.807 1.00 34.18 . 1 66 ATOM C CG LYS A 15 . −11.000 −12.324 45.176 1.00 38.29 . 1 67 ATOM C CD LYS A 15 . −11.907 −11.826 44.013 1.00 41.47 . 1 68 ATOM C CE LYS A 15 . −13.275 −11.280 44.493 1.00 42.02 . 1 69 ATOM N NZ LYS A 15 . −13.778 −10.258 43.502 1.00 39.40 . 1 70 ATOM N N ALA A 16 . −10.687 −9.313 45.260 1.00 28.50 . 1 71 ATOM C CA ALA A 16 . −11.628 −8.263 44.869 1.00 27.17 . 1 72 ATOM C C ALA A 16 . −10.855 −6.953 44.699 1.00 25.65 . 1 73 ATOM O O ALA A 16 . −11.168 −6.147 43.809 1.00 22.74 . 1 74 ATOM C CB ALA A 16 . −12.723 −8.102 45.934 1.00 27.89 . 1 75 ATOM N N GLN A 17 . −9.851 −6.750 45.556 1.00 24.14 . 1 76 ATOM C CA GLN A 17 . −9.060 −5.517 45.463 1.00 23.39 . 1 77 ATOM C C GLN A 17 . −8.318 −5.484 44.123 1.00 23.05 . 1 78 ATOM O O GLN A 17 . −8.246 −4.446 43.470 1.00 22.53 . 1 79 ATOM C CB GLN A 17 . −8.051 −5.397 46.653 1.00 24.10 . 1 80 ATOM C CG GLN A 17 . −7.243 −4.046 46.562 1.00 25.91 . 1 81 ATOM C CD GLN A 17 . −6.372 −3.760 47.775 1.00 28.67 . 1 82 ATOM O OE1 GLN A 17 . −6.019 −4.675 48.519 1.00 27.38 . 1 83 ATOM N NE2 GLN A 17 . −5.996 −2.468 47.974 1.00 28.04 . 1 84 ATOM N N ALA A 18 . −7.766 −6.632 43.716 1.00 22.32 . 1 85 ATOM C CA ALA A 18 . −7.027 −6.730 42.459 1.00 23.07 . 1 86 ATOM C C ALA A 18 . −7.973 −6.376 41.294 1.00 22.60 . 1 87 ATOM O O ALA A 18 . −7.605 −5.612 40.398 1.00 21.85 . 1 88 ATOM C CB ALA A 18 . −6.434 −8.126 42.301 1.00 23.04 . 1 89 ATOM N N LEU A 19 . −9.212 −6.878 41.357 1.00 21.92 . 1 90 ATOM C CA LEU A 19 . −10.219 −6.565 40.357 1.00 22.66 . 1 91 ATOM C C LEU A 19 . −10.525 −5.067 40.315 1.00 22.64 . 1 92 ATOM O O LEU A 19 . −10.566 −4.470 39.246 1.00 20.73 . 1 93 ATOM C CB LEU A 19 . −11.513 −7.349 40.644 1.00 26.12 . 1 94 ATOM C CG LEU A 19 . −12.598 −7.091 39.620 1.00 25.96 . 1 95 ATOM C CD1 LEU A 19 . −12.091 −7.552 38.233 1.00 28.92 . 1 96 ATOM C CD2 LEU A 19 . −13.895 −7.845 40.015 1.00 28.66 . 1 97 ATOM N N LEU A 20 . −10.769 −4.479 41.485 1.00 21.05 . 1 98 ATOM C CA LEU A 20 . −11.062 −3.050 41.577 1.00 23.00 . 1 99 ATOM C C LEU A 20 . −9.921 −2.233 40.973 1.00 23.27 . 1 100 ATOM O O LEU A 20 . −10.153 −1.318 40.155 1.00 21.84 . 1 101 ATOM C CB LEU A 20 . −11.273 −2.609 43.035 1.00 22.45 . 1 102 ATOM C CG LEU A 20 . −11.536 −1.087 43.191 1.00 24.97 . 1 103 ATOM C CD1 LEU A 20 . −12.928 −0.772 42.593 1.00 26.15 . 1 104 ATOM C CD2 LEU A 20 . −11.530 −0.704 44.697 1.00 24.19 . 1 105 ATOM N N TYR A 21 . −8.695 −2.563 41.346 1.00 22.84 . 1 106 ATOM C CA TYR A 21 . −7.553 −1.847 40.788 1.00 24.14 . 1 107 ATOM C C TYR A 21 . −7.440 −1.994 39.284 1.00 23.62 . 1 108 ATOM O O TYR A 21 . −7.079 −1.033 38.592 1.00 21.76 . 1 109 ATOM C CB TYR A 21 . −6.246 −2.326 41.419 1.00 25.44 . 1 110 ATOM C CG TYR A 21 . −5.926 −1.712 42.758 1.00 26.14 . 1 111 ATOM C CD1 TYR A 21 . −6.913 −1.293 43.631 1.00 27.63 . 1 112 ATOM C CD2 TYR A 21 . −4.595 −1.602 43.164 1.00 28.87 . 1 113 ATOM C CE1 TYR A 21 . −6.586 −0.773 44.891 1.00 29.10 . 1 114 ATOM C CE2 TYR A 21 . −4.256 −1.086 44.418 1.00 29.87 . 1 115 ATOM C CZ TYR A 21 . −5.252 −0.671 45.266 1.00 30.24 . 1 116 ATOM O OH TYR A 21 . −4.874 −0.098 46.478 1.00 33.92 . 1 117 ATOM N N LYS A 22 . −7.719 −3.187 38.764 1.00 22.90 . 1 118 ATOM C CA LYS A 22 . −7.642 −3.372 37.306 1.00 23.15 . 1 119 ATOM C C LYS A 22 . −8.568 −2.359 36.592 1.00 22.81 . 1 120 ATOM O O LYS A 22 . −8.198 −1.809 35.558 1.00 23.35 . 1 121 ATOM C CB LYS A 22 . −8.026 −4.839 36.929 1.00 26.29 . 1 122 ATOM C CG LYS A 22 . −8.247 −5.109 35.432 1.00 29.66 . 1 123 ATOM C CD LYS A 22 . −8.448 −6.616 35.197 1.00 32.95 . 1 124 ATOM C CE LYS A 22 . −8.678 −6.905 33.702 1.00 37.61 . 1 125 ATOM N NZ LYS A 22 . −8.844 −8.361 33.427 1.00 39.38 . 1 126 ATOM N N HIS A 23 . −9.738 −2.080 37.185 1.00 21.02 . 1 127 ATOM C CA HIS A 23 . −10.683 −1.159 36.561 1.00 20.90 . 1 128 ATOM C C HIS A 23 . −10.432 0.266 36.872 1.00 19.51 . 1 129 ATOM O O HIS A 23 . −10.627 1.138 36.007 1.00 20.08 . 1 130 ATOM C CB HIS A 23 . −12.121 −1.618 36.891 1.00 21.91 . 1 131 ATOM C CG HIS A 23 . −12.487 −2.877 36.169 1.00 25.26 . 1 132 ATOM N ND1 HIS A 23 . −12.149 −4.137 36.622 1.00 25.78 . 1 133 ATOM C CD2 HIS A 23 . −13.057 −3.056 34.953 1.00 23.25 . 1 134 ATOM C CE1 HIS A 23 . −12.499 −5.039 35.713 1.00 27.13 . 1 135 ATOM N NE2 HIS A 23 . −13.046 −4.405 34.691 1.00 27.11 . 1 136 ATOM N N ILE A 24 . −9.984 0.562 38.086 1.00 19.72 . 1 137 ATOM C CA ILE A 24 . −9.684 1.969 38.362 1.00 20.87 . 1 138 ATOM C C ILE A 24 . −8.627 2.437 37.352 1.00 21.82 . 1 139 ATOM O O ILE A 24 . −8.738 3.532 36.780 1.00 22.48 . 1 140 ATOM C CB ILE A 24 . −9.055 2.125 39.769 1.00 20.82 . 1 141 ATOM C CG1 ILE A 24 . −10.140 1.979 40.815 1.00 22.13 . 1 142 ATOM C CG2 ILE A 24 . −8.405 3.550 39.950 1.00 19.09 . 1 143 ATOM C CD1 ILE A 24 . −9.534 1.947 42.279 1.00 23.11 . 1 144 ATOM N N TYR A 25 . −7.622 1.589 37.121 1.00 21.67 . 1 145 ATOM C CA TYR A 25 . −6.509 1.978 36.255 1.00 20.85 . 1 146 ATOM C C TYR A 25 . −6.608 1.541 34.806 1.00 20.17 . 1 147 ATOM O O TYR A 25 . −5.623 1.637 34.046 1.00 20.03 . 1 148 ATOM C CB TYR A 25 . −5.168 1.500 36.882 1.00 22.05 . 1 149 ATOM C CG TYR A 25 . −4.886 2.165 38.212 1.00 23.57 . 1 150 ATOM C CD1 TYR A 25 . −5.140 1.503 39.423 1.00 24.52 . 1 151 ATOM C CD2 TYR A 25 . −4.375 3.455 38.270 1.00 23.24 . 1 152 ATOM C CE1 TYR A 25 . −4.873 2.119 40.644 1.00 26.08 . 1 153 ATOM C CE2 TYR A 25 . −4.118 4.080 39.490 1.00 24.44 . 1 154 ATOM C CZ TYR A 25 . −4.369 3.404 40.668 1.00 27.08 . 1 155 ATOM O OH TYR A 25 . −4.182 4.016 41.895 1.00 28.46 . 1 156 ATOM N N ALA A 26 . −7.795 1.108 34.393 1.00 19.42 . 1 157 ATOM C CA ALA A 26 . −7.952 0.656 33.007 1.00 20.17 . 1 158 ATOM C C ALA A 26 . −7.593 1.739 31.980 1.00 20.39 . 1 159 ATOM O O ALA A 26 . −7.133 1.405 30.865 1.00 20.63 . 1 160 ATOM C CB ALA A 26 . −9.394 0.148 32.778 1.00 21.48 . 1 161 ATOM N N PHE A 27 . −7.796 3.028 32.317 1.00 20.48 . 1 162 ATOM C CA PHE A 27 . −7.446 4.122 31.414 1.00 21.17 . 1 163 ATOM C C PHE A 27 . −5.990 4.071 30.970 1.00 22.65 . 1 164 ATOM O O PHE A 27 . −5.664 4.588 29.896 1.00 20.68 . 1 165 ATOM C CB PHE A 27 . −7.779 5.499 32.004 1.00 21.87 . 1 166 ATOM C CG PHE A 27 . −6.911 5.924 33.166 1.00 23.33 . 1 167 ATOM C CD1 PHE A 27 . −5.769 6.694 32.942 1.00 22.00 . 1 168 ATOM C CD2 PHE A 27 . −7.213 5.523 34.483 1.00 22.74 . 1 169 ATOM C CE1 PHE A 27 . −4.927 7.063 34.004 1.00 23.89 . 1 170 ATOM C CE2 PHE A 27 . −6.352 5.894 35.564 1.00 24.72 . 1 171 ATOM C CZ PHE A 27 . −5.203 6.675 35.302 1.00 22.90 . 1 172 ATOM N N ILE A 28 . −5.122 3.455 31.792 1.00 20.62 . 1 173 ATOM C CA ILE A 28 . −3.712 3.336 31.395 1.00 22.74 . 1 174 ATOM C C ILE A 28 . −3.563 2.422 30.161 1.00 21.81 . 1 175 ATOM O O ILE A 28 . −2.628 2.608 29.389 1.00 22.54 . 1 176 ATOM C CB ILE A 28 . −2.846 2.821 32.564 1.00 23.75 . 1 177 ATOM C CG1 ILE A 28 . −2.846 3.873 33.658 1.00 23.38 . 1 178 ATOM C CG2 ILE A 28 . −1.428 2.575 32.147 1.00 24.20 . 1 179 ATOM C CD1 ILE A 28 . −1.915 3.560 34.812 1.00 27.67 . 1 180 ATOM N N ASP A 29 . −4.477 1.476 29.939 1.00 22.30 . 1 181 ATOM C CA ASP A 29 . −4.383 0.640 28.717 1.00 22.38 . 1 182 ATOM C C ASP A 29 . −4.546 1.588 27.531 1.00 22.35 . 1 183 ATOM O O ASP A 29 . −3.774 1.539 26.539 1.00 22.92 . 1 184 ATOM C CB ASP A 29 . −5.497 −0.412 28.625 1.00 24.52 . 1 185 ATOM C CG ASP A 29 . −5.131 −1.706 29.332 1.00 29.74 . 1 186 ATOM O OD1 ASP A 29 . −3.914 −1.881 29.614 1.00 28.54 . 1 187 ATOM O OD2 ASP A 29 . −6.054 −2.531 29.610 1.00 29.37 . 1 188 ATOM N N SER A 30 . −5.541 2.465 27.620 1.00 21.99 . 1 189 ATOM C CA SER A 30 . −5.826 3.413 26.534 1.00 20.79 . 1 190 ATOM C C SER A 30 . −4.717 4.435 26.361 1.00 20.86 . 1 191 ATOM O O SER A 30 . −4.258 4.674 25.238 1.00 21.11 . 1 192 ATOM C CB SER A 30 . −7.145 4.166 26.770 1.00 21.58 . 1 193 ATOM O OG SER A 30 . −8.252 3.256 26.886 1.00 19.85 . 1 194 HETA N N MSE A 31 . −4.247 4.985 27.466 1.00 19.60 . 1 195 HETA C CA MSE A 31 . −3.205 5.997 27.385 1.00 17.94 . 1 196 HETA C C MSE A 31 . −1.839 5.500 26.913 1.00 18.69 . 1 197 HETA O O MSE A 31 . −1.074 6.258 26.274 1.00 19.67 . 1 198 HETA C CB MSE A 31 . −3.081 6.724 28.723 1.00 18.78 . 1 199 HETA C CG MSE A 31 . −4.363 7.460 29.133 1.00 19.63 . 1 200 HETA SE SE MSE A 31 . −4.750 8.950 27.901 1.00 10.56 . 1 201 HETA C CE MSE A 31 . −6.079 7.945 26.743 1.00 19.86 . 1 202 ATOM N N SER A 32 . −1.519 4.243 27.252 1.00 18.87 . 1 203 ATOM C CA SER A 32 . −0.241 3.656 26.841 1.00 20.45 . 1 204 ATOM C C SER A 32 . −0.293 3.341 25.316 1.00 20.78 . 1 205 ATOM O O SER A 32 . 0.718 3.513 24.604 1.00 20.34 . 1 206 ATOM C CB SER A 32 . 0.061 2.386 27.663 1.00 22.45 . 1 207 ATOM O OG SER A 32 . −0.901 1.373 27.437 1.00 22.78 . 1 208 ATOM N N LEU A 33 . −1.458 2.899 24.843 1.00 20.12 . 1 209 ATOM C CA LEU A 33 . −1.634 2.622 23.417 1.00 19.45 . 1 210 ATOM C C LEU A 33 . −1.506 3.938 22.662 1.00 20.08 . 1 211 ATOM O O LEU A 33 . −0.876 4.002 21.594 1.00 19.53 . 1 212 ATOM C CB LEU A 33 . −3.032 2.021 23.172 1.00 19.06 . 1 213 ATOM C CG LEU A 33 . −3.473 1.796 21.717 1.00 17.36 . 1 214 ATOM C CD1 LEU A 33 . −2.450 0.961 21.007 1.00 21.69 . 1 215 ATOM C CD2 LEU A 33 . −4.896 1.164 21.693 1.00 21.34 . 1 216 ATOM N N LYS A 34 . −2.159 4.988 23.172 1.00 19.45 . 1 217 ATOM C CA LYS A 34 . −2.066 6.314 22.536 1.00 20.27 . 1 218 ATOM C C LYS A 34 . −0.620 6.783 22.468 1.00 19.30 . 1 219 ATOM O O LYS A 34 . −0.200 7.302 21.438 1.00 20.05 . 1 220 ATOM C CB LYS A 34 . −2.889 7.314 23.309 1.00 19.79 . 1 221 ATOM C CG LYS A 34 . −2.743 8.806 22.877 1.00 20.78 . 1 222 ATOM C CD LYS A 34 . −3.596 9.715 23.704 1.00 21.49 . 1 223 ATOM C CE LYS A 34 . −3.225 11.161 23.407 1.00 21.68 . 1 224 ATOM N NZ LYS A 34 . −4.278 12.214 23.661 1.00 21.43 . 1 225 ATOM N N TRP A 35 . 0.137 6.551 23.551 1.00 18.93 . 1 226 ATOM C CA TRP A 35 . 1.552 6.923 23.592 1.00 19.32 . 1 227 ATOM C C TRP A 35 . 2.323 6.186 22.505 1.00 20.59 . 1 228 ATOM O O TRP A 35 . 3.190 6.766 21.823 1.00 21.15 . 1 229 ATOM C CB TRP A 35 . 2.117 6.593 25.017 1.00 20.02 . 1 230 ATOM C CG TRP A 35 . 3.612 6.729 25.116 1.00 20.36 . 1 231 ATOM C CD1 TRP A 35 . 4.324 7.872 25.298 1.00 20.15 . 1 232 ATOM C CD2 TRP A 35 . 4.554 5.677 25.028 1.00 18.48 . 1 233 ATOM N NE1 TRP A 35 . 5.672 7.596 25.343 1.00 19.80 . 1 234 ATOM C CE2 TRP A 35 . 5.843 6.254 25.180 1.00 19.05 . 1 235 ATOM C CE3 TRP A 35 . 4.450 4.317 24.822 1.00 20.80 . 1 236 ATOM C CZ2 TRP A 35 . 7.014 5.500 25.142 1.00 20.93 . 1 237 ATOM C CZ3 TRP A 35 . 5.620 3.552 24.770 1.00 20.99 . 1 238 ATOM C CH2 TRP A 35 . 6.898 4.155 24.932 1.00 21.71 . 1 239 ATOM N N ALA A 36 . 2.053 4.884 22.353 1.00 19.17 . 1 240 ATOM C CA ALA A 36 . 2.798 4.159 21.349 1.00 19.45 . 1 241 ATOM C C ALA A 36 . 2.564 4.708 19.948 1.00 19.70 . 1 242 ATOM O O ALA A 36 . 3.490 4.766 19.127 1.00 20.35 . 1 243 ATOM C CB ALA A 36 . 2.494 2.663 21.423 1.00 18.33 . 1 244 ATOM N N VAL A 37 . 1.345 5.118 19.669 1.00 19.31 . 1 245 ATOM C CA VAL A 37 . 1.040 5.675 18.365 1.00 19.77 . 1 246 ATOM C C VAL A 37 . 1.688 7.051 18.186 1.00 19.09 . 1 247 ATOM O O VAL A 37 . 2.282 7.302 17.139 1.00 20.80 . 1 248 ATOM C CB VAL A 37 . −0.471 5.770 18.187 1.00 18.42 . 1 249 ATOM C CG1 VAL A 37 . −0.829 6.636 16.938 1.00 20.26 . 1 250 ATOM C CG2 VAL A 37 . −1.020 4.340 18.014 1.00 18.52 . 1 251 ATOM N N GLU A 38 . 1.627 7.900 19.227 1.00 20.21 . 1 252 ATOM C CA GLU A 38 . 2.197 9.242 19.179 1.00 20.39 . 1 253 ATOM C C GLU A 38 . 3.733 9.225 19.014 1.00 20.85 . 1 254 ATOM O O GLU A 38 . 4.280 10.097 18.366 1.00 21.22 . 1 255 ATOM C CB GLU A 38 . 1.831 10.080 20.417 1.00 21.17 . 1 256 ATOM C CG GLU A 38 . 0.341 10.415 20.553 1.00 23.57 . 1 257 ATOM C CD GLU A 38 . 0.047 11.609 21.471 1.00 24.90 . 1 258 ATOM O OE1 GLU A 38 . 0.729 11.747 22.521 1.00 21.86 . 1 259 ATOM O OE2 GLU A 38 . −0.886 12.420 21.161 1.00 24.66 . 1 260 HETA N N MSE A 39 . 4.392 8.230 19.604 1.00 20.21 . 1 261 HETA C CA MSE A 39 . 5.853 8.090 19.490 1.00 20.69 . 1 262 HETA C C MSE A 39 . 6.240 7.458 18.144 1.00 20.87 . 1 263 HETA O O MSE A 39 . 7.428 7.371 17.805 1.00 22.48 . 1 264 HETA C CB MSE A 39 . 6.385 7.217 20.656 1.00 20.06 . 1 265 HETA C CG MSE A 39 . 6.128 7.778 22.030 1.00 19.66 . 1 266 HETA SE SE MSE A 39 . 7.082 9.333 22.365 1.00 16.65 . 1 267 HETA C CE MSE A 39 . 8.855 8.618 22.486 1.00 22.74 . 1 268 ATOM N N ASN A 40 . 5.228 6.977 17.397 1.00 19.63 . 1 269 ATOM C CA ASN A 40 . 5.388 6.378 16.076 1.00 21.85 . 1 270 ATOM C C ASN A 40 . 6.138 5.069 16.131 1.00 21.69 . 1 271 ATOM O O ASN A 40 . 6.815 4.688 15.205 1.00 22.39 . 1 272 ATOM C CB ASN A 40 . 6.125 7.350 15.164 1.00 21.04 . 1 273 ATOM C CG ASN A 40 . 5.922 7.031 13.701 1.00 22.01 . 1 274 ATOM O OD1 ASN A 40 . 6.835 7.158 12.920 1.00 28.10 . 1 275 ATOM N ND2 ASN A 40 . 4.713 6.604 13.337 1.00 22.62 . 1 276 ATOM N N ILE A 41 . 5.986 4.362 17.248 1.00 21.58 . 1 277 ATOM C CA ILE A 41 . 6.692 3.106 17.438 1.00 21.72 . 1 278 ATOM C C ILE A 41 . 6.356 1.984 16.446 1.00 21.05 . 1 279 ATOM O O ILE A 41 . 7.270 1.311 15.921 1.00 21.45 . 1 280 ATOM C CB ILE A 41 . 6.589 2.728 18.946 1.00 19.99 . 1 281 ATOM C CG1 ILE A 41 . 7.454 3.743 19.716 1.00 19.97 . 1 282 ATOM C CG2 ILE A 41 . 7.143 1.325 19.199 1.00 22.65 . 1 283 ATOM C CD1 ILE A 41 . 7.244 3.743 21.266 1.00 17.94 . 1 284 ATOM N N PRO A 42 . 5.069 1.762 16.139 1.00 21.72 . 1 285 ATOM C CA PRO A 42 . 4.744 0.702 15.182 1.00 21.48 . 1 286 ATOM C C PRO A 42 . 5.465 0.932 13.862 1.00 22.52 . 1 287 ATOM O O PRO A 42 . 6.123 0.033 13.324 1.00 22.79 . 1 288 ATOM C CB PRO A 42 . 3.217 0.841 15.015 1.00 21.56 . 1 289 ATOM C CG PRO A 42 . 2.788 1.143 16.467 1.00 20.31 . 1 290 ATOM C CD PRO A 42 . 3.885 2.158 16.925 1.00 21.54 . 1 291 ATOM N N ASN A 43 . 5.365 2.153 13.340 1.00 23.02 . 1 292 ATOM C CA ASN A 43 . 6.048 2.414 12.084 1.00 24.12 . 1 293 ATOM C C ASN A 43 . 7.578 2.301 12.216 1.00 23.51 . 1 294 ATOM O O ASN A 43 . 8.233 1.866 11.261 1.00 23.11 . 1 295 ATOM C CB ASN A 43 . 5.662 3.798 11.547 1.00 24.79 . 1 296 ATOM C CG ASN A 43 . 4.238 3.847 11.020 1.00 23.25 . 1 297 ATOM O OD1 ASN A 43 . 3.541 4.872 11.124 1.00 28.55 . 1 298 ATOM N ND2 ASN A 43 . 3.816 2.784 10.427 1.00 28.43 . 1 299 ATOM N N ILE A 44 . 8.151 2.676 13.362 1.00 22.50 . 1 300 ATOM C CA ILE A 44 . 9.603 2.575 13.534 1.00 22.50 . 1 301 ATOM C C ILE A 44 . 10.043 1.111 13.448 1.00 22.05 . 1 302 ATOM O O ILE A 44 . 11.044 0.796 12.784 1.00 22.64 . 1 303 ATOM C CB ILE A 44 . 10.062 3.220 14.880 1.00 22.41 . 1 304 ATOM C CG1 ILE A 44 . 10.019 4.768 14.747 1.00 23.15 . 1 305 ATOM C CG2 ILE A 44 . 11.460 2.746 15.287 1.00 21.46 . 1 306 ATOM C CD1 ILE A 44 . 10.057 5.474 16.157 1.00 24.09 . 1 307 ATOM N N ILE A 45 . 9.240 0.223 14.039 1.00 22.98 . 1 308 ATOM C CA ILE A 45 . 9.570 −1.189 14.032 1.00 23.22 . 1 309 ATOM C C ILE A 45 . 9.418 −1.754 12.649 1.00 24.53 . 1 310 ATOM O O ILE A 45 . 10.291 −2.518 12.184 1.00 23.61 . 1 311 ATOM C CB ILE A 45 . 8.765 −1.958 15.096 1.00 22.17 . 1 312 ATOM C CG1 ILE A 45 . 9.187 −1.483 16.495 1.00 23.80 . 1 313 ATOM C CG2 ILE A 45 . 9.069 −3.444 15.028 1.00 22.63 . 1 314 ATOM C CD1 ILE A 45 . 8.408 −2.183 17.661 1.00 23.06 . 1 315 ATOM N N GLN A 46 . 8.327 −1.387 11.976 1.00 24.49 . 1 316 ATOM C CA GLN A 46 . 8.093 −1.845 10.604 1.00 26.19 . 1 317 ATOM C C GLN A 46 . 9.294 −1.463 9.728 1.00 26.58 . 1 318 ATOM O O GLN A 46 . 9.857 −2.295 9.003 1.00 27.60 . 1 319 ATOM C CB GLN A 46 . 6.835 −1.181 10.039 1.00 26.84 . 1 320 ATOM C CG GLN A 46 . 6.567 −1.471 8.566 1.00 29.62 . 1 321 ATOM C CD GLN A 46 . 6.245 −2.960 8.320 1.00 33.63 . 1 322 ATOM O OE1 GLN A 46 . 5.634 −3.620 9.170 1.00 35.42 . 1 323 ATOM N NE2 GLN A 46 . 6.641 −3.478 7.156 1.00 35.17 . 1 324 ATOM N N ASN A 47 . 9.669 −0.185 9.794 1.00 26.88 . 1 325 ATOM C CA ASN A 47 . 10.780 0.337 8.994 1.00 25.27 . 1 326 ATOM C C ASN A 47 . 12.132 −0.287 9.310 1.00 26.33 . 1 327 ATOM O O ASN A 47 . 13.002 −0.339 8.452 1.00 25.64 . 1 328 ATOM C CB ASN A 47 . 10.854 1.841 9.158 1.00 26.85 . 1 329 ATOM C CG ASN A 47 . 9.626 2.532 8.626 1.00 27.28 . 1 330 ATOM O OD1 ASN A 47 . 9.369 3.684 8.960 1.00 33.03 . 1 331 ATOM N ND2 ASN A 47 . 8.883 1.859 7.784 1.00 29.45 . 1 332 ATOM N N HIS A 48 . 12.295 −0.763 10.542 1.00 24.10 . 1 333 ATOM C CA HIS A 48 . 13.508 −1.407 10.990 1.00 24.97 . 1 334 ATOM C C HIS A 48 . 13.675 −2.757 10.281 1.00 24.79 . 1 335 ATOM O O HIS A 48 . 14.811 −3.199 10.012 1.00 26.25 . 1 336 ATOM C CB HIS A 48 . 13.429 −1.603 12.498 1.00 23.40 . 1 337 ATOM C CG HIS A 48 . 14.716 −2.020 13.128 1.00 25.27 . 1 338 ATOM N ND1 HIS A 48 . 15.900 −1.339 12.932 1.00 26.65 . 1 339 ATOM C CD2 HIS A 48 . 14.987 −3.002 14.015 1.00 24.50 . 1 340 ATOM C CE1 HIS A 48 . 16.844 −1.894 13.669 1.00 28.22 . 1 341 ATOM N NE2 HIS A 48 . 16.317 −2.910 14.333 1.00 25.50 . 1 342 ATOM N N GLY A 49 . 12.544 −3.403 9.995 1.00 26.80 . 1 343 ATOM C CA GLY A 49 . 12.536 −4.665 9.275 1.00 25.69 . 1 344 ATOM C C GLY A 49 . 12.767 −5.945 10.073 1.00 27.71 . 1 345 ATOM O O GLY A 49 . 12.811 −7.048 9.520 1.00 29.73 . 1 346 ATOM N N LYS A 50 . 12.955 −5.794 11.371 1.00 27.80 . 1 347 ATOM C CA LYS A 50 . 13.188 −6.910 12.268 1.00 27.33 . 1 348 ATOM C C LYS A 50 . 12.869 −6.383 13.654 1.00 27.08 . 1 349 ATOM O O LYS A 50 . 12.637 −5.191 13.824 1.00 27.21 . 1 350 ATOM C CB LYS A 50 . 14.655 −7.333 12.202 1.00 28.77 . 1 351 ATOM C CG LYS A 50 . 15.666 −6.292 12.706 1.00 30.78 . 1 352 ATOM C CD LYS A 50 . 17.077 −6.867 12.581 1.00 35.55 . 1 353 ATOM C CE LYS A 50 . 18.107 −5.967 13.201 1.00 37.50 . 1 354 ATOM N NZ LYS A 50 . 18.959 −5.347 12.128 1.00 40.46 . 1 355 ATOM N N PRO A 51 . 12.845 −7.257 14.671 1.00 27.17 . 1 356 ATOM C CA PRO A 51 . 12.544 −6.759 16.029 1.00 26.91 . 1 357 ATOM C C PRO A 51 . 13.588 −5.735 16.447 1.00 26.71 . 1 358 ATOM O O PRO A 51 . 14.781 −5.900 16.178 1.00 25.90 . 1 359 ATOM C CB PRO A 51 . 12.603 −8.024 16.892 1.00 27.71 . 1 360 ATOM C CG PRO A 51 . 12.147 −9.088 15.913 1.00 28.06 . 1 361 ATOM C CD PRO A 51 . 12.829 −8.729 14.625 1.00 27.75 . 1 362 ATOM N N ILE A 52 . 13.150 −4.674 17.117 1.00 25.41 . 1 363 ATOM C CA ILE A 52 . 14.097 −3.664 17.491 1.00 24.82 . 1 364 ATOM C C ILE A 52 . 14.572 −3.737 18.925 1.00 25.04 . 1 365 ATOM O O ILE A 52 . 13.774 −3.926 19.862 1.00 25.43 . 1 366 ATOM C CB ILE A 52 . 13.498 −2.300 17.176 1.00 24.98 . 1 367 ATOM C CG1 ILE A 52 . 14.580 −1.239 17.093 1.00 26.59 . 1 368 ATOM C CG2 ILE A 52 . 12.429 −1.952 18.220 1.00 24.51 . 1 369 ATOM C CD1 ILE A 52 . 14.057 0.054 16.553 1.00 25.82 . 1 370 ATOM N N SER A 53 . 15.867 −3.542 19.133 1.00 24.62 . 1 371 ATOM C CA SER A 53 . 16.355 −3.617 20.496 1.00 24.25 . 1 372 ATOM C C SER A 53 . 15.998 −2.362 21.260 1.00 23.17 . 1 373 ATOM O O SER A 53 . 15.837 −1.268 20.668 1.00 23.26 . 1 374 ATOM C CB SER A 53 . 17.876 −3.786 20.514 1.00 22.80 . 1 375 ATOM O OG SER A 53 . 18.495 −2.646 19.899 1.00 25.27 . 1 376 ATOM N N LEU A 54 . 15.897 −2.492 22.586 1.00 23.68 . 1 377 ATOM C CA LEU A 54 . 15.600 −1.316 23.385 1.00 24.40 . 1 378 ATOM C C LEU A 54 . 16.596 −0.181 23.121 1.00 24.05 . 1 379 ATOM O O LEU A 54 . 16.221 0.991 23.061 1.00 24.93 . 1 380 ATOM C CB LEU A 54 . 15.598 −1.641 24.898 1.00 24.90 . 1 381 ATOM C CG LEU A 54 . 15.365 −0.415 25.809 1.00 24.88 . 1 382 ATOM C CD1 LEU A 54 . 13.893 0.075 25.692 1.00 26.76 . 1 383 ATOM C CD2 LEU A 54 . 15.672 −0.764 27.260 1.00 28.61 . 1 384 ATOM N N SER A 55 . 17.873 −0.517 22.949 1.00 26.14 . 1 385 ATOM C CA SER A 55 . 18.868 0.520 22.726 1.00 27.16 . 1 386 ATOM C C SER A 55 . 18.685 1.303 21.429 1.00 26.75 . 1 387 ATOM O O SER A 55 . 18.863 2.526 21.405 1.00 26.76 . 1 388 ATOM C CB SER A 55 . 20.289 −0.091 22.797 1.00 29.58 . 1 389 ATOM O OG SER A 55 . 20.609 −0.798 21.610 1.00 32.53 . 1 390 ATOM N N ASN A 56 . 18.320 0.605 20.354 1.00 26.55 . 1 391 ATOM C CA ASN A 56 . 18.124 1.235 19.051 1.00 26.49 . 1 392 ATOM C C ASN A 56 . 16.810 1.999 19.064 1.00 26.13 . 1 393 ATOM O O ASN A 56 . 16.694 3.079 18.465 1.00 27.16 . 1 394 ATOM C CB ASN A 56 . 18.111 0.186 17.933 1.00 27.31 . 1 395 ATOM C CG ASN A 56 . 19.487 −0.195 17.492 1.00 27.15 . 1 396 ATOM O OD1 ASN A 56 . 20.425 0.598 17.640 1.00 29.12 . 1 397 ATOM N ND2 ASN A 56 . 19.623 −1.376 16.910 1.00 27.47 . 1 398 ATOM N N LEU A 57 . 15.818 1.436 19.756 1.00 25.32 . 1 399 ATOM C CA LEU A 57 . 14.525 2.112 19.837 1.00 24.67 . 1 400 ATOM C C LEU A 57 . 14.680 3.480 20.505 1.00 26.16 . 1 401 ATOM O O LEU A 57 . 14.258 4.499 19.946 1.00 26.85 . 1 402 ATOM C CB LEU A 57 . 13.520 1.263 20.628 1.00 24.22 . 1 403 ATOM C CG LEU A 57 . 12.203 2.018 20.831 1.00 22.13 . 1 404 ATOM C CD1 LEU A 57 . 11.629 2.336 19.418 1.00 23.07 . 1 405 ATOM C CD2 LEU A 57 . 11.199 1.156 21.662 1.00 25.09 . 1 406 ATOM N N VAL A 58 . 15.270 3.534 21.695 1.00 26.90 . 1 407 ATOM C CA VAL A 58 . 15.400 4.822 22.373 1.00 27.39 . 1 408 ATOM C C VAL A 58 . 16.412 5.714 21.634 1.00 28.02 . 1 409 ATOM O O VAL A 58 . 16.379 6.935 21.767 1.00 27.34 . 1 410 ATOM C CB VAL A 58 . 15.766 4.682 23.885 1.00 28.22 . 1 411 ATOM C CG1 VAL A 58 . 14.697 3.812 24.638 1.00 29.18 . 1 412 ATOM C CG2 VAL A 58 . 17.175 4.106 24.022 1.00 29.78 . 1 413 ATOM N N SER A 59 . 17.300 5.096 20.851 1.00 27.31 . 1 414 ATOM C CA SER A 59 . 18.254 5.876 20.073 1.00 29.56 . 1 415 ATOM C C SER A 59 . 17.465 6.622 19.013 1.00 29.67 . 1 416 ATOM O O SER A 59 . 17.635 7.833 18.830 1.00 29.45 . 1 417 ATOM C CB SER A 59 . 19.289 4.999 19.390 1.00 29.73 . 1 418 ATOM O OG SER A 59 . 20.156 5.871 18.687 1.00 34.28 . 1 419 ATOM N N ILE A 60 . 16.594 5.905 18.308 1.00 28.20 . 1 420 ATOM C CA ILE A 60 . 15.748 6.544 17.301 1.00 27.90 . 1 421 ATOM C C ILE A 60 . 14.827 7.624 17.920 1.00 26.92 . 1 422 ATOM O O ILE A 60 . 14.693 8.723 17.381 1.00 27.92 . 1 423 ATOM C CB ILE A 60 . 14.897 5.495 16.551 1.00 27.50 . 1 424 ATOM C CG1 ILE A 60 . 15.836 4.458 15.915 1.00 26.46 . 1 425 ATOM C CG2 ILE A 60 . 13.930 6.200 15.552 1.00 25.04 . 1 426 ATOM C CD1 ILE A 60 . 15.175 3.463 15.004 1.00 28.41 . 1 427 ATOM N N LEU A 61 . 14.186 7.306 19.045 1.00 25.97 . 1 428 ATOM C CA LEU A 61 . 13.303 8.235 19.721 1.00 25.36 . 1 429 ATOM C C LEU A 61 . 14.006 9.462 20.317 1.00 24.82 . 1 430 ATOM O O LEU A 61 . 13.387 10.524 20.457 1.00 25.47 . 1 431 ATOM C CB LEU A 61 . 12.521 7.494 20.828 1.00 25.18 . 1 432 ATOM C CG LEU A 61 . 11.597 6.368 20.340 1.00 26.15 . 1 433 ATOM C CD1 LEU A 61 . 10.952 5.663 21.511 1.00 25.53 . 1 434 ATOM C CD2 LEU A 61 . 10.477 6.983 19.509 1.00 24.08 . 1 435 ATOM N N GLN A 62 . 15.295 9.328 20.632 1.00 26.00 . 1 436 ATOM C CA GLN A 62 . 16.085 10.416 21.220 1.00 26.57 . 1 437 ATOM C C GLN A 62 . 15.506 10.907 22.544 1.00 26.44 . 1 438 ATOM O O GLN A 62 . 15.465 12.105 22.844 1.00 26.86 . 1 439 ATOM C CB GLN A 62 . 16.212 11.569 20.222 1.00 29.13 . 1 440 ATOM C CG GLN A 62 . 17.164 11.242 19.078 1.00 33.14 . 1 441 ATOM C CD GLN A 62 . 18.637 11.233 19.537 1.00 35.36 . 1 442 ATOM O OE1 GLN A 62 . 19.192 12.293 19.913 1.00 37.98 . 1 443 ATOM N NE2 GLN A 62 . 19.269 10.047 19.533 1.00 36.70 . 1 444 ATOM N N VAL A 63 . 15.041 9.956 23.339 1.00 26.55 . 1 445 ATOM C CA VAL A 63 . 14.494 10.271 24.653 1.00 26.99 . 1 446 ATOM C C VAL A 63 . 15.730 10.455 25.558 1.00 26.66 . 1 447 ATOM O O VAL A 63 . 16.818 9.898 25.288 1.00 27.23 . 1 448 ATOM C CB VAL A 63 . 13.626 9.089 25.248 1.00 28.34 . 1 449 ATOM C CG1 VAL A 63 . 12.425 8.766 24.333 1.00 27.91 . 1 450 ATOM C CG2 VAL A 63 . 14.481 7.858 25.418 1.00 28.07 . 1 451 ATOM N N PRO A 64 . 15.576 11.240 26.632 1.00 26.85 . 1 452 ATOM C CA PRO A 64 . 16.687 11.478 27.572 1.00 27.58 . 1 453 ATOM C C PRO A 64 . 17.046 10.186 28.311 1.00 27.37 . 1 454 ATOM O O PRO A 64 . 16.198 9.367 28.571 1.00 25.46 . 1 455 ATOM C CB PRO A 64 . 16.133 12.560 28.484 1.00 27.75 . 1 456 ATOM C CG PRO A 64 . 14.658 12.463 28.329 1.00 28.45 . 1 457 ATOM C CD PRO A 64 . 14.439 12.122 26.925 1.00 27.02 . 1 458 ATOM N N SER A 65 . 18.320 9.998 28.655 1.00 27.27 . 1 459 ATOM C CA SER A 65 . 18.696 8.736 29.308 1.00 28.11 . 1 460 ATOM C C SER A 65 . 17.888 8.430 30.589 1.00 26.27 . 1 461 ATOM O O SER A 65 . 17.666 7.256 30.942 1.00 26.16 . 1 462 ATOM C CB SER A 65 . 20.176 8.786 29.632 1.00 30.58 . 1 463 ATOM O OG SER A 65 . 20.423 9.944 30.395 1.00 36.07 . 1 464 ATOM N N SER A 66 . 17.485 9.488 31.276 1.00 25.82 . 1 465 ATOM C CA SER A 66 . 16.721 9.366 32.504 1.00 26.07 . 1 466 ATOM C C SER A 66 . 15.327 8.791 32.283 1.00 24.52 . 1 467 ATOM O O SER A 66 . 14.661 8.459 33.266 1.00 25.03 . 1 468 ATOM C CB SER A 66 . 16.555 10.709 33.205 1.00 26.97 . 1 469 ATOM O OG SER A 66 . 15.709 11.579 32.462 1.00 28.92 . 1 470 ATOM N N LYS A 67 . 14.888 8.699 31.027 1.00 25.55 . 1 471 ATOM C CA LYS A 67 . 13.560 8.175 30.737 1.00 25.11 . 1 472 ATOM C C LYS A 67 . 13.583 6.872 29.941 1.00 24.46 . 1 473 ATOM O O LYS A 67 . 12.526 6.347 29.586 1.00 22.66 . 1 474 ATOM C CB LYS A 67 . 12.738 9.236 29.987 1.00 25.59 . 1 475 ATOM C CG LYS A 67 . 12.386 10.429 30.829 1.00 24.67 . 1 476 ATOM C CD LYS A 67 . 11.279 10.066 31.881 1.00 23.99 . 1 477 ATOM C CE LYS A 67 . 11.006 11.129 32.957 1.00 25.32 . 1 478 ATOM N NZ LYS A 67 . 10.537 12.478 32.505 1.00 22.65 . 1 479 ATOM N N ILE A 68 . 14.768 6.340 29.669 1.00 22.52 . 1 480 ATOM C CA ILE A 68 . 14.884 5.077 28.929 1.00 23.55 . 1 481 ATOM C C ILE A 68 . 14.200 3.929 29.668 1.00 23.39 . 1 482 ATOM O O ILE A 68 . 13.493 3.104 29.063 1.00 23.36 . 1 483 ATOM C CB ILE A 68 . 16.406 4.750 28.652 1.00 23.40 . 1 484 ATOM C CG1 ILE A 68 . 16.930 5.719 27.570 1.00 25.06 . 1 485 ATOM C CG2 ILE A 68 . 16.558 3.321 28.225 1.00 24.78 . 1 486 ATOM C CD1 ILE A 68 . 18.467 5.720 27.384 1.00 27.36 . 1 487 ATOM N N GLY A 69 . 14.404 3.861 30.982 1.00 23.80 . 1 488 ATOM C CA GLY A 69 . 13.753 2.801 31.739 1.00 23.44 . 1 489 ATOM C C GLY A 69 . 12.251 2.886 31.682 1.00 23.03 . 1 490 ATOM O O GLY A 69 . 11.539 1.874 31.678 1.00 21.88 . 1 491 ATOM N N ASN A 70 . 11.765 4.121 31.640 1.00 22.96 . 1 492 ATOM C CA ASN A 70 . 10.340 4.374 31.536 1.00 23.54 . 1 493 ATOM C C ASN A 70 . 9.837 3.891 30.163 1.00 22.42 . 1 494 ATOM O O ASN A 70 . 8.702 3.388 30.049 1.00 23.90 . 1 495 ATOM C CB ASN A 70 . 10.104 5.848 31.740 1.00 21.97 . 1 496 ATOM C CG ASN A 70 . 10.191 6.261 33.222 1.00 21.03 . 1 497 ATOM O OD1 ASN A 70 . 9.345 5.866 34.045 1.00 27.55 . 1 498 ATOM N ND2 ASN A 70 . 11.195 7.027 33.569 1.00 19.30 . 1 499 ATOM N N VAL A 71 . 10.657 4.043 29.124 1.00 22.51 . 1 500 ATOM C CA VAL A 71 . 10.244 3.551 27.823 1.00 21.03 . 1 501 ATOM C C VAL A 71 . 10.147 2.041 27.920 1.00 21.65 . 1 502 ATOM O O VAL A 71 . 9.196 1.419 27.465 1.00 19.93 . 1 503 ATOM C CB VAL A 71 . 11.296 3.922 26.737 1.00 20.31 . 1 504 ATOM C CG1 VAL A 71 . 11.038 3.118 25.472 1.00 21.01 . 1 505 ATOM C CG2 VAL A 71 . 11.183 5.403 26.418 1.00 21.53 . 1 506 ATOM N N ARG A 72 . 11.163 1.421 28.510 1.00 21.78 . 1 507 ATOM C CA ARG A 72 . 11.146 −0.028 28.637 1.00 22.44 . 1 508 ATOM C C ARG A 72 . 9.909 −0.502 29.396 1.00 21.57 . 1 509 ATOM O O ARG A 72 . 9.271 −1.481 28.994 1.00 21.45 . 1 510 ATOM C CB ARG A 72 . 12.391 −0.518 29.401 1.00 23.61 . 1 511 ATOM C CG ARG A 72 . 12.436 −2.034 29.577 1.00 27.58 . 1 512 ATOM C CD ARG A 72 . 13.662 −2.555 30.350 1.00 30.45 . 1 513 ATOM N NE ARG A 72 . 13.986 −1.741 31.517 1.00 36.21 . 1 514 ATOM C CZ ARG A 72 . 13.183 −1.492 32.551 1.00 37.79 . 1 515 ATOM N NH1 ARG A 72 . 11.944 −2.003 32.625 1.00 42.06 . 1 516 ATOM N NH2 ARG A 72 . 13.602 −0.662 33.498 1.00 39.31 . 1 517 ATOM N N ARG A 73 . 9.574 0.177 30.484 1.00 22.50 . 1 518 ATOM C CA ARG A 73 . 8.421 −0.258 31.275 1.00 21.92 . 1 519 ATOM C C ARG A 73 . 7.119 −0.169 30.480 1.00 21.81 . 1 520 ATOM O O ARG A 73 . 6.244 −1.041 30.564 1.00 22.02 . 1 521 ATOM C CB ARG A 73 . 8.368 0.570 32.569 1.00 20.26 . 1 522 ATOM C CG ARG A 73 . 9.431 0.130 33.608 1.00 24.10 . 1 523 ATOM C CD ARG A 73 . 9.960 1.244 34.520 1.00 25.36 . 1 524 ATOM N NE ARG A 73 . 9.052 1.771 35.561 1.00 30.76 . 1 525 ATOM C CZ ARG A 73 . 9.259 2.855 36.350 1.00 30.97 . 1 526 ATOM N NH1 ARG A 73 . 10.371 3.646 36.290 1.00 33.61 . 1 527 ATOM N NH2 ARG A 73 . 8.313 3.168 37.224 1.00 27.80 . 1 528 ATOM N N LEU A 74 . 7.007 0.878 29.701 1.00 20.91 . 1 529 ATOM C CA LEU A 74 . 5.807 1.057 28.875 1.00 20.96 . 1 530 ATOM C C LEU A 74 . 5.734 −0.004 27.779 1.00 21.21 . 1 531 ATOM O O LEU A 74 . 4.643 −0.555 27.521 1.00 21.36 . 1 532 ATOM C CB LEU A 74 . 5.811 2.474 28.291 1.00 20.35 . 1 533 ATOM C CG LEU A 74 . 5.316 3.578 29.227 1.00 20.54 . 1 534 ATOM C CD1 LEU A 74 . 5.643 4.972 28.683 1.00 20.96 . 1 535 ATOM C CD2 LEU A 74 . 3.818 3.490 29.349 1.00 20.96 . 1 536 HETA N N MSE A 75 . 6.885 −0.292 27.148 1.00 18.78 . 1 537 HETA C CA MSE A 75 . 6.929 −1.277 26.085 1.00 21.22 . 1 538 HETA C C MSE A 75 . 6.589 −2.671 26.597 1.00 21.37 . 1 539 HETA O O MSE A 75 . 5.915 −3.452 25.909 1.00 22.30 . 1 540 HETA C CB MSE A 75 . 8.279 −1.287 25.379 1.00 19.60 . 1 541 HETA C CG MSE A 75 . 8.543 −0.048 24.573 1.00 22.49 . 1 542 HETA SE SE MSE A 75 . 7.302 0.116 23.079 1.00 12.46 . 1 543 HETA C CE MSE A 75 . 7.803 −1.597 22.074 1.00 21.78 . 1 544 ATOM N N ARG A 76 . 6.994 −2.959 27.818 1.00 22.56 . 1 545 ATOM C CA ARG A 76 . 6.715 −4.269 28.375 1.00 23.84 . 1 546 ATOM C C ARG A 76 . 5.244 −4.421 28.698 1.00 22.79 . 1 547 ATOM O O ARG A 76 . 4.664 −5.497 28.529 1.00 23.22 . 1 548 ATOM C CB ARG A 76 . 7.579 −4.502 29.606 1.00 22.58 . 1 549 ATOM C CG ARG A 76 . 9.006 −4.766 29.215 1.00 25.99 . 1 550 ATOM C CD ARG A 76 . 9.840 −4.886 30.465 1.00 29.88 . 1 551 ATOM N NE ARG A 76 . 11.187 −5.356 30.211 1.00 29.67 . 1 552 ATOM C CZ ARG A 76 . 11.950 −5.945 31.138 1.00 32.54 . 1 553 ATOM N NH1 ARG A 76 . 11.496 −6.142 32.390 1.00 32.60 . 1 554 ATOM N NH2 ARG A 76 . 13.198 −6.314 30.821 1.00 33.82 . 1 555 ATOM N N TYR A 77 . 4.669 −3.330 29.175 1.00 22.46 . 1 556 ATOM C CA TYR A 77 . 3.244 −3.282 29.504 1.00 20.68 . 1 557 ATOM C C TYR A 77 . 2.443 −3.451 28.209 1.00 22.14 . 1 558 ATOM O O TYR A 77 . 1.475 −4.229 28.177 1.00 21.39 . 1 559 ATOM C CB TYR A 77 . 2.941 −1.950 30.173 1.00 19.85 . 1 560 ATOM C CG TYR A 77 . 1.486 −1.782 30.567 1.00 21.26 . 1 561 ATOM C CD1 TYR A 77 . 0.983 −2.381 31.730 1.00 24.39 . 1 562 ATOM C CD2 TYR A 77 . 0.612 −1.017 29.803 1.00 22.81 . 1 563 ATOM C CE1 TYR A 77 . −0.360 −2.200 32.126 1.00 26.00 . 1 564 ATOM C CE2 TYR A 77 . −0.743 −0.849 30.190 1.00 23.98 . 1 565 ATOM C CZ TYR A 77 . −1.214 −1.427 31.332 1.00 26.04 . 1 566 ATOM O OH TYR A 77 . −2.546 −1.299 31.710 1.00 26.98 . 1 567 ATOM N N LEU A 78 . 2.825 −2.718 27.141 1.00 20.46 . 1 568 ATOM C CA LEU A 78 . 2.117 −2.858 25.848 1.00 22.06 . 1 569 ATOM C C LEU A 78 . 2.298 −4.247 25.235 1.00 22.24 . 1 570 ATOM O O LEU A 78 . 1.396 −4.756 24.575 1.00 23.98 . 1 571 ATOM C CB LEU A 78 . 2.553 −1.787 24.849 1.00 22.69 . 1 572 ATOM C CG LEU A 78 . 2.108 −0.340 25.123 1.00 22.36 . 1 573 ATOM C CD1 LEU A 78 . 3.160 0.661 24.587 1.00 23.45 . 1 574 ATOM C CD2 LEU A 78 . 0.749 −0.139 24.478 1.00 24.89 . 1 575 ATOM N N ALA A 79 . 3.461 −4.854 25.467 1.00 21.69 . 1 576 ATOM C CA ALA A 79 . 3.736 −6.205 24.949 1.00 23.07 . 1 577 ATOM C C ALA A 79 . 2.821 −7.206 25.644 1.00 24.36 . 1 578 ATOM O O ALA A 79 . 2.234 −8.078 25.015 1.00 25.09 . 1 579 ATOM C CB ALA A 79 . 5.230 −6.591 25.181 1.00 23.10 . 1 580 ATOM N N HIS A 80 . 2.684 −7.070 26.951 1.00 24.51 . 1 581 ATOM C CA HIS A 80 . 1.856 −7.999 27.672 1.00 26.01 . 1 582 ATOM C C HIS A 80 . 0.403 −7.881 27.184 1.00 25.93 . 1 583 ATOM O O HIS A 80 . −0.329 −8.862 27.173 1.00 27.56 . 1 584 ATOM C CB HIS A 80 . 1.937 −7.738 29.170 1.00 26.69 . 1 585 ATOM C CG HIS A 80 . 1.227 −8.781 29.967 1.00 29.59 . 1 586 ATOM N ND1 HIS A 80 . −0.042 −8.588 30.478 1.00 31.14 . 1 587 ATOM C CD2 HIS A 80 . 1.539 −10.080 30.197 1.00 29.76 . 1 588 ATOM C CE1 HIS A 80 . −0.483 −9.730 30.988 1.00 32.20 . 1 589 ATOM N NE2 HIS A 80 . 0.457 −10.648 30.828 1.00 33.06 . 1 590 ATOM N N ASN A 81 . −0.006 −6.693 26.771 1.00 24.61 . 1 591 ATOM C CA ASN A 81 . −1.361 −6.534 26.248 1.00 25.32 . 1 592 ATOM C C ASN A 81 . −1.533 −7.082 24.837 1.00 25.68 . 1 593 ATOM O O ASN A 81 . −2.664 −7.194 24.358 1.00 27.26 . 1 594 ATOM C CB ASN A 81 . −1.786 −5.077 26.283 1.00 24.76 . 1 595 ATOM C CG ASN A 81 . −2.208 −4.648 27.680 1.00 26.90 . 1 596 ATOM O OD1 ASN A 81 . −2.567 −5.487 28.497 1.00 28.11 . 1 597 ATOM N ND2 ASN A 81 . −2.173 −3.353 27.951 1.00 26.91 . 1 598 ATOM N N GLY A 82 . −0.436 −7.413 24.182 1.00 23.77 . 1 599 ATOM C CA GLY A 82 . −0.531 −7.995 22.858 1.00 24.54 . 1 600 ATOM C C GLY A 82 . −0.129 −7.126 21.700 1.00 23.43 . 1 601 ATOM O O GLY A 82 . −0.291 −7.525 20.535 1.00 24.30 . 1 602 ATOM N N PHE A 83 . 0.418 −5.965 21.992 1.00 22.83 . 1 603 ATOM C CA PHE A 83 . 0.795 −5.073 20.918 1.00 21.94 . 1 604 ATOM C C PHE A 83 . 2.196 −5.219 20.456 1.00 21.61 . 1 605 ATOM O O PHE A 83 . 2.556 −4.649 19.452 1.00 22.05 . 1 606 ATOM C CB PHE A 83 . 0.531 −3.622 21.329 1.00 20.84 . 1 607 ATOM C CG PHE A 83 . −0.911 −3.344 21.472 1.00 23.78 . 1 608 ATOM C CD1 PHE A 83 . −1.508 −3.361 22.722 1.00 22.86 . 1 609 ATOM C CD2 PHE A 83 . −1.704 −3.196 20.340 1.00 24.45 . 1 610 ATOM C CE1 PHE A 83 . −2.890 −3.237 22.863 1.00 24.19 . 1 611 ATOM C CE2 PHE A 83 . −3.085 −3.071 20.470 1.00 25.51 . 1 612 ATOM C CZ PHE A 83 . −3.679 −3.091 21.720 1.00 23.62 . 1 613 ATOM N N PHE A 84 . 2.999 −5.977 21.199 1.00 22.23 . 1 614 ATOM C CA PHE A 84 . 4.360 −6.254 20.787 1.00 22.26 . 1 615 ATOM C C PHE A 84 . 4.738 −7.626 21.285 1.00 23.56 . 1 616 ATOM O O PHE A 84 . 4.120 −8.142 22.217 1.00 23.89 . 1 617 ATOM C CB PHE A 84 . 5.358 −5.263 21.370 1.00 24.29 . 1 618 ATOM C CG PHE A 84 . 5.105 −3.845 20.922 1.00 23.40 . 1 619 ATOM C CD1 PHE A 84 . 4.610 −2.905 21.803 1.00 25.40 . 1 620 ATOM C CD2 PHE A 84 . 5.293 −3.484 19.560 1.00 23.79 . 1 621 ATOM C CE1 PHE A 84 . 4.290 −1.601 21.345 1.00 24.54 . 1 622 ATOM C CE2 PHE A 84 . 4.994 −2.226 19.090 1.00 24.61 . 1 623 ATOM C CZ PHE A 84 . 4.488 −1.259 19.968 1.00 25.23 . 1 624 ATOM N N GLU A 85 . 5.764 −8.208 20.674 1.00 24.50 . 1 625 ATOM C CA GLU A 85 . 6.232 −9.493 21.145 1.00 26.86 . 1 626 ATOM C C GLU A 85 . 7.648 −9.248 21.629 1.00 27.47 . 1 627 ATOM O O GLU A 85 . 8.487 −8.664 20.890 1.00 28.02 . 1 628 ATOM C CB GLU A 85 . 6.233 −10.518 20.022 1.00 27.82 . 1 629 ATOM C CG GLU A 85 . 6.858 −11.831 20.454 1.00 33.19 . 1 630 ATOM C CD GLU A 85 . 7.073 −12.753 19.307 1.00 36.76 . 1 631 ATOM O OE1 GLU A 85 . 6.898 −12.312 18.140 1.00 37.57 . 1 632 ATOM O OE2 GLU A 85 . 7.425 −13.925 19.569 1.00 38.95 . 1 633 ATOM N N ILE A 86 . 7.950 −9.667 22.850 1.00 26.68 . 1 634 ATOM C CA ILE A 86 . 9.326 −9.484 23.319 1.00 29.31 . 1 635 ATOM C C ILE A 86 . 10.136 −10.697 22.878 1.00 30.91 . 1 636 ATOM O O ILE A 86 . 9.702 −11.855 23.064 1.00 31.32 . 1 637 ATOM C CB ILE A 86 . 9.416 −9.324 24.862 1.00 30.03 . 1 638 ATOM C CG1 ILE A 86 . 8.705 −8.032 25.269 1.00 29.32 . 1 639 ATOM C CG2 ILE A 86 . 10.894 −9.215 25.311 1.00 30.40 . 1 640 ATOM C CD1 ILE A 86 . 8.492 −7.868 26.714 1.00 32.19 . 1 641 ATOM N N ILE A 87 . 11.290 −10.416 22.277 1.00 32.83 . 1 642 ATOM C CA ILE A 87 . 12.216 −11.435 21.795 1.00 36.09 . 1 643 ATOM C C ILE A 87 . 13.530 −11.154 22.525 1.00 37.68 . 1 644 ATOM O O ILE A 87 . 14.121 −10.092 22.365 1.00 37.79 . 1 645 ATOM C CB ILE A 87 . 12.371 −11.340 20.256 1.00 36.84 . 1 646 ATOM C CG1 ILE A 87 . 11.027 −11.685 19.594 1.00 37.40 . 1 647 ATOM C CG2 ILE A 87 . 13.460 −12.316 19.759 1.00 37.94 . 1 648 ATOM C CD1 ILE A 87 . 10.992 −11.453 18.102 1.00 39.89 . 1 649 ATOM N N THR A 88 . 13.993 −12.113 23.327 1.00 40.21 . 1 650 ATOM C CA THR A 88 . 15.216 −11.896 24.109 1.00 42.37 . 1 651 ATOM C C THR A 88 . 16.435 −12.673 23.651 1.00 42.99 . 1 652 ATOM O O THR A 88 . 16.391 −13.893 23.505 1.00 43.52 . 1 653 ATOM C CB THR A 88 . 14.993 −12.242 25.588 1.00 43.14 . 1 654 ATOM O OG1 THR A 88 . 13.850 −11.529 26.075 1.00 44.71 . 1 655 ATOM C CG2 THR A 88 . 16.212 −11.841 26.427 1.00 43.26 . 1 656 ATOM N N LYS A 89 . 17.521 −11.937 23.425 1.00 44.76 . 1 657 ATOM C CA LYS A 89 . 18.796 −12.517 23.007 1.00 45.69 . 1 658 ATOM C C LYS A 89 . 19.814 −11.810 23.897 1.00 45.83 . 1 659 ATOM O O LYS A 89 . 19.730 −11.863 25.114 1.00 46.28 . 1 660 ATOM C CB LYS A 89 . 19.106 −12.187 21.544 1.00 46.63 . 1 661 ATOM C CG LYS A 89 . 17.908 −12.132 20.607 1.00 47.25 . 1 662 ATOM C CD LYS A 89 . 17.348 −13.516 20.316 1.00 47.48 . 1 663 ATOM C CE LYS A 89 . 17.202 −13.703 18.814 1.00 48.12 . 1 664 ATOM N NZ LYS A 89 . 16.531 −14.983 18.440 1.00 48.48 . 1 665 ATOM N N GLU A 90 . 20.772 −11.131 23.288 1.00 46.47 . 1 666 ATOM C CA GLU A 90 . 21.753 −10.434 24.085 1.00 46.75 . 1 667 ATOM C C GLU A 90 . 21.090 −9.164 24.592 1.00 45.77 . 1 668 ATOM O O GLU A 90 . 21.510 −8.559 25.591 1.00 46.69 . 1 669 ATOM C CB GLU A 90 . 22.998 −10.128 23.247 1.00 49.16 . 1 670 ATOM C CG GLU A 90 . 24.178 −11.072 23.526 1.00 51.33 . 1 671 ATOM C CD GLU A 90 . 24.678 −10.999 24.974 1.00 53.46 . 1 672 ATOM O OE1 GLU A 90 . 25.726 −11.634 25.275 1.00 54.59 . 1 673 ATOM O OE2 GLU A 90 . 24.027 −10.312 25.812 1.00 54.47 . 1 674 ATOM N N GLU A 91 . 20.033 −8.764 23.901 1.00 43.92 . 1 675 ATOM C CA GLU A 91 . 19.291 −7.588 24.312 1.00 41.69 . 1 676 ATOM C C GLU A 91 . 17.838 −7.983 24.260 1.00 39.16 . 1 677 ATOM O O GLU A 91 . 17.480 −9.019 23.715 1.00 38.97 . 1 678 ATOM C CB GLU A 91 . 19.491 −6.389 23.347 1.00 43.19 . 1 679 ATOM C CG GLU A 91 . 20.688 −5.463 23.637 1.00 45.08 . 1 680 ATOM C CD GLU A 91 . 20.477 −4.021 23.151 1.00 46.28 . 1 681 ATOM O OE1 GLU A 91 . 19.590 −3.294 23.713 1.00 46.82 . 1 682 ATOM O OE2 GLU A 91 . 21.201 −3.610 22.218 1.00 45.61 . 1 683 ATOM N N GLU A 92 . 16.999 −7.149 24.849 1.00 36.84 . 1 684 ATOM C CA GLU A 92 . 15.576 −7.389 24.767 1.00 33.48 . 1 685 ATOM C C GLU A 92 . 15.161 −6.643 23.495 1.00 31.76 . 1 686 ATOM O O GLU A 92 . 15.591 −5.504 23.287 1.00 31.77 . 1 687 ATOM C CB GLU A 92 . 14.891 −6.796 25.986 1.00 34.39 . 1 688 ATOM C CG GLU A 92 . 13.383 −6.705 25.859 1.00 32.97 . 1 689 ATOM C CD GLU A 92 . 12.723 −6.473 27.186 1.00 33.44 . 1 690 ATOM O OE1 GLU A 92 . 12.884 −7.361 28.056 1.00 32.94 . 1 691 ATOM O OE2 GLU A 92 . 12.048 −5.414 27.354 1.00 34.66 . 1 692 ATOM N N SER A 93 . 14.377 −7.287 22.639 1.00 28.35 . 1 693 ATOM C CA SER A 93 . 13.896 −6.618 21.429 1.00 27.24 . 1 694 ATOM C C SER A 93 . 12.381 −6.737 21.278 1.00 26.24 . 1 695 ATOM O O SER A 93 . 11.720 −7.608 21.867 1.00 26.12 . 1 696 ATOM C CB SER A 93 . 14.601 −7.146 20.189 1.00 28.99 . 1 697 ATOM O OG SER A 93 . 15.983 −6.924 20.336 1.00 30.87 . 1 698 ATOM N N TYR A 94 . 11.829 −5.831 20.487 1.00 25.03 . 1 699 ATOM C CA TYR A 94 . 10.372 −5.795 20.313 1.00 23.72 . 1 700 ATOM C C TYR A 94 . 9.920 −5.988 18.872 1.00 25.01 . 1 701 ATOM O O TYR A 94 . 10.393 −5.290 17.970 1.00 24.70 . 1 702 ATOM C CB TYR A 94 . 9.811 −4.443 20.842 1.00 23.71 . 1 703 ATOM C CG TYR A 94 . 10.337 −4.050 22.222 1.00 22.95 . 1 704 ATOM C CD1 TYR A 94 . 11.438 −3.178 22.366 1.00 24.64 . 1 705 ATOM C CD2 TYR A 94 . 9.810 −4.639 23.374 1.00 23.60 . 1 706 ATOM C CE1 TYR A 94 . 11.988 −2.917 23.600 1.00 24.93 . 1 707 ATOM C CE2 TYR A 94 . 10.361 −4.398 24.617 1.00 23.64 . 1 708 ATOM C CZ TYR A 94 . 11.430 −3.540 24.729 1.00 24.98 . 1 709 ATOM O OH TYR A 94 . 11.925 −3.235 25.955 1.00 26.37 . 1 710 ATOM N N ALA A 95 . 8.998 −6.935 18.651 1.00 23.83 . 1 711 ATOM C CA ALA A 95 . 8.483 −7.195 17.332 1.00 24.56 . 1 712 ATOM C C ALA A 95 . 7.010 −6.781 17.305 1.00 24.72 . 1 713 ATOM O O ALA A 95 . 6.327 −6.743 18.344 1.00 23.81 . 1 714 ATOM C CB ALA A 95 . 8.599 −8.713 16.994 1.00 25.62 . 1 715 ATOM N N LEU A 96 . 6.523 −6.506 16.095 1.00 25.77 . 1 716 ATOM C CA LEU A 96 . 5.118 −6.162 15.910 1.00 25.39 . 1 717 ATOM C C LEU A 96 . 4.323 −7.455 16.038 1.00 25.21 . 1 718 ATOM O O LEU A 96 . 4.893 −8.560 15.964 1.00 24.20 . 1 719 ATOM C CB LEU A 96 . 4.874 −5.568 14.530 1.00 28.25 . 1 720 ATOM C CG LEU A 96 . 5.410 −4.150 14.293 1.00 30.74 . 1 721 ATOM C CD1 LEU A 96 . 4.890 −3.656 12.927 1.00 33.57 . 1 722 ATOM C CD2 LEU A 96 . 4.979 −3.221 15.413 1.00 30.97 . 1 723 ATOM N N THR A 97 . 3.022 −7.296 16.254 1.00 23.81 . 1 724 ATOM C CA THR A 97 . 2.092 −8.401 16.352 1.00 25.86 . 1 725 ATOM C C THR A 97 . 0.987 −7.984 15.353 1.00 26.23 . 1 726 ATOM O O THR A 97 . 1.007 −6.866 14.823 1.00 26.60 . 1 727 ATOM C CB THR A 97 . 1.467 −8.531 17.782 1.00 25.78 . 1 728 ATOM O OG1 THR A 97 . 0.693 −7.360 18.105 1.00 27.62 . 1 729 ATOM C CG2 THR A 97 . 2.534 −8.699 18.806 1.00 25.93 . 1 730 ATOM N N VAL A 98 . 0.035 −8.870 15.085 1.00 26.39 . 1 731 ATOM C CA VAL A 98 . −1.048 −8.527 14.167 1.00 27.22 . 1 732 ATOM C C VAL A 98 . −1.802 −7.271 14.633 1.00 26.13 . 1 733 ATOM O O VAL A 98 . −2.184 −6.445 13.817 1.00 24.59 . 1 734 ATOM C CB VAL A 98 . −2.026 −9.710 14.008 1.00 27.89 . 1 735 ATOM C CG1 VAL A 98 . −3.108 −9.382 13.031 1.00 28.68 . 1 736 ATOM C CG2 VAL A 98 . −1.287 −10.911 13.495 1.00 29.43 . 1 737 ATOM N N ALA A 99 . −2.010 −7.138 15.947 1.00 25.83 . 1 738 ATOM C CA ALA A 99 . −2.704 −5.959 16.486 1.00 25.14 . 1 739 ATOM C C ALA A 99 . −1.921 −4.668 16.249 1.00 26.05 . 1 740 ATOM O O ALA A 99 . −2.527 −3.628 15.923 1.00 24.60 . 1 741 ATOM C CB ALA A 99 . −2.984 −6.147 17.986 1.00 25.97 . 1 742 ATOM N N SER A 100 . −0.590 −4.689 16.399 1.00 24.14 . 1 743 ATOM C CA SER A 100 . 0.149 −3.444 16.155 1.00 24.80 . 1 744 ATOM C C SER A 100 . 0.416 −3.221 14.686 1.00 24.02 . 1 745 ATOM O O SER A 100 . 0.760 −2.114 14.287 1.00 23.26 . 1 746 ATOM C CB SER A 100 . 1.447 −3.393 16.954 1.00 24.71 . 1 747 ATOM O OG SER A 100 . 2.222 −4.563 16.824 1.00 23.69 . 1 748 ATOM N N GLU A 101 . 0.232 −4.259 13.868 1.00 24.65 . 1 749 ATOM C CA GLU A 101 . 0.395 −4.078 12.430 1.00 25.02 . 1 750 ATOM C C GLU A 101 . −0.809 −3.242 11.957 1.00 24.10 . 1 751 ATOM O O GLU A 101 . −0.768 −2.600 10.910 1.00 23.93 . 1 752 ATOM C CB GLU A 101 . 0.419 −5.437 11.701 1.00 29.01 . 1 753 ATOM C CG GLU A 101 . 1.780 −6.153 11.735 1.00 32.48 . 1 754 ATOM C CD GLU A 101 . 1.696 −7.598 11.199 1.00 36.02 . 1 755 ATOM O OE1 GLU A 101 . 0.669 −7.963 10.584 1.00 39.21 . 1 756 ATOM O OE2 GLU A 101 . 2.658 −8.368 11.383 1.00 40.25 . 1 757 ATOM N N LEU A 102 . −1.891 −3.243 12.741 1.00 23.67 . 1 758 ATOM C CA LEU A 102 . −3.082 −2.455 12.385 1.00 24.53 . 1 759 ATOM C C LEU A 102 . −2.726 −0.987 12.630 1.00 22.84 . 1 760 ATOM O O LEU A 102 . −3.521 −0.078 12.366 1.00 24.02 . 1 761 ATOM C CB LEU A 102 . −4.306 −2.821 13.292 1.00 23.68 . 1 762 ATOM C CG LEU A 102 . −4.988 −4.212 13.243 1.00 25.54 . 1 763 ATOM C CD1 LEU A 102 . −5.979 −4.377 14.392 1.00 26.31 . 1 764 ATOM C CD2 LEU A 102 . −5.683 −4.381 11.908 1.00 26.96 . 1 765 ATOM N N LEU A 103 . −1.542 −0.740 13.171 1.00 22.08 . 1 766 ATOM C CA LEU A 103 . −1.156 0.647 13.474 1.00 22.15 . 1 767 ATOM C C LEU A 103 . −0.113 1.215 12.518 1.00 22.50 . 1 768 ATOM O O LEU A 103 . 0.249 2.368 12.633 1.00 21.51 . 1 769 ATOM C CB LEU A 103 . −0.659 0.752 14.932 1.00 21.57 . 1 770 ATOM C CG LEU A 103 . −1.699 0.340 16.007 1.00 22.32 . 1 771 ATOM C CD1 LEU A 103 . −1.051 0.308 17.421 1.00 21.93 . 1 772 ATOM C CD2 LEU A 103 . −2.906 1.304 16.009 1.00 24.88 . 1 773 ATOM N N VAL A 104 . 0.345 0.378 11.588 1.00 22.37 . 1 774 ATOM C CA VAL A 104 . 1.371 0.726 10.625 1.00 24.47 . 1 775 ATOM C C VAL A 104 . 0.812 1.436 9.389 1.00 27.74 . 1 776 ATOM O O VAL A 104 . −0.104 0.940 8.691 1.00 26.12 . 1 777 ATOM C CB VAL A 104 . 2.128 −0.531 10.233 1.00 24.65 . 1 778 ATOM C CG1 VAL A 104 . 3.134 −0.249 9.086 1.00 25.21 . 1 779 ATOM C CG2 VAL A 104 . 2.865 −1.085 11.448 1.00 25.64 . 1 780 ATOM N N ARG A 105 . 1.352 2.618 9.147 1.00 29.47 . 1 781 ATOM C CA ARG A 105 . 0.933 3.428 8.016 1.00 34.82 . 1 782 ATOM C C ARG A 105 . 0.876 2.659 6.699 1.00 37.24 . 1 783 ATOM O O ARG A 105 . 1.743 1.843 6.393 1.00 38.06 . 1 784 ATOM C CB ARG A 105 . 1.902 4.599 7.850 1.00 37.13 . 1 785 ATOM C CG ARG A 105 . 1.492 5.677 6.837 1.00 40.56 . 1 786 ATOM C CD ARG A 105 . 2.682 6.588 6.547 1.00 43.64 . 1 787 ATOM N NE ARG A 105 . 3.349 7.024 7.778 1.00 46.66 . 1 788 ATOM C CZ ARG A 105 . 2.716 7.512 8.845 1.00 48.29 . 1 789 ATOM N NH1 ARG A 105 . 1.391 7.629 8.851 1.00 49.75 . 1 790 ATOM N NH2 ARG A 105 . 3.405 7.891 9.913 1.00 48.33 . 1 791 ATOM N N GLY A 106 . −0.153 2.941 5.916 1.00 39.13 . 1 792 ATOM C CA GLY A 106 . −0.263 2.321 4.613 1.00 42.64 . 1 793 ATOM C C GLY A 106 . −0.242 0.805 4.579 1.00 44.42 . 1 794 ATOM O O GLY A 106 . 0.189 0.197 3.592 1.00 46.05 . 1 795 ATOM N N SER A 107 . −0.673 0.190 5.669 1.00 45.08 . 1 796 ATOM C CA SER A 107 . −0.768 −1.248 5.723 1.00 45.71 . 1 797 ATOM C C SER A 107 . −2.165 −1.296 5.125 1.00 45.40 . 1 798 ATOM O O SER A 107 . −2.752 −0.236 4.893 1.00 46.37 . 1 799 ATOM C CB SER A 107 . −0.785 −1.717 7.171 1.00 46.36 . 1 800 ATOM O OG SER A 107 . −2.010 −1.343 7.784 1.00 47.55 . 1 801 ATOM N N ASP A 108 . −2.702 −2.484 4.868 1.00 45.11 . 1 802 ATOM C CA ASP A 108 . −4.043 −2.590 4.281 1.00 44.16 . 1 803 ATOM C C ASP A 108 . −5.126 −1.901 5.126 1.00 42.22 . 1 804 ATOM O O ASP A 108 . −5.869 −1.068 4.617 1.00 43.31 . 1 805 ATOM C CB ASP A 108 . −4.396 −4.068 4.066 1.00 46.22 . 1 806 ATOM C CG ASP A 108 . −4.029 −4.567 2.674 1.00 47.46 . 1 807 ATOM O OD1 ASP A 108 . −3.279 −3.882 1.936 1.00 48.95 . 1 808 ATOM O OD2 ASP A 108 . −4.503 −5.662 2.316 1.00 48.69 . 1 809 ATOM N N LEU A 109 . −5.230 −2.268 6.406 1.00 39.55 . 1 810 ATOM C CA LEU A 109 . −6.185 −1.665 7.334 1.00 34.67 . 1 811 ATOM C C LEU A 109 . −5.335 −0.985 8.405 1.00 32.96 . 1 812 ATOM O O LEU A 109 . −4.706 −1.676 9.212 1.00 33.68 . 1 813 ATOM C CB LEU A 109 . −7.059 −2.735 8.009 1.00 35.08 . 1 814 ATOM C CG LEU A 109 . −8.053 −2.243 9.076 1.00 35.92 . 1 815 ATOM C CD1 LEU A 109 . −9.064 −1.269 8.437 1.00 36.59 . 1 816 ATOM C CD2 LEU A 109 . −8.773 −3.455 9.707 1.00 37.70 . 1 817 ATOM N N CYS A 110 . −5.288 0.346 8.402 1.00 27.61 . 1 818 ATOM C CA CYS A 110 . −4.486 1.083 9.398 1.00 26.03 . 1 819 ATOM C C CYS A 110 . −5.455 1.877 10.236 1.00 25.51 . 1 820 ATOM O O CYS A 110 . −6.105 2.849 9.727 1.00 24.22 . 1 821 ATOM C CB CYS A 110 . −3.539 2.073 8.740 1.00 26.16 . 1 822 ATOM S SG CYS A 110 . −2.582 3.003 9.985 1.00 26.16 . 1 823 ATOM N N LEU A 111 . −5.536 1.499 11.509 1.00 23.92 . 1 824 ATOM C CA LEU A 111 . −6.495 2.123 12.405 1.00 24.10 . 1 825 ATOM C C LEU A 111 . −5.924 3.134 13.353 1.00 22.96 . 1 826 ATOM O O LEU A 111 . −6.620 3.574 14.258 1.00 24.50 . 1 827 ATOM C CB LEU A 111 . −7.272 1.020 13.173 1.00 25.37 . 1 828 ATOM C CG LEU A 111 . −7.989 0.091 12.208 1.00 28.23 . 1 829 ATOM C CD1 LEU A 111 . −8.633 −1.066 12.958 1.00 26.86 . 1 830 ATOM C CD2 LEU A 111 . −9.030 0.947 11.397 1.00 27.74 . 1 831 ATOM N N ALA A 112 . −4.657 3.486 13.165 1.00 22.15 . 1 832 ATOM C CA ALA A 112 . −4.019 4.454 14.057 1.00 22.55 . 1 833 ATOM C C ALA A 112 . −4.816 5.755 14.128 1.00 23.45 . 1 834 ATOM O O ALA A 112 . −4.951 6.328 15.211 1.00 24.63 . 1 835 ATOM C CB ALA A 112 . −2.556 4.736 13.640 1.00 23.62 . 1 836 ATOM N N PRO A 113 . −5.402 6.240 13.011 1.00 22.66 . 1 837 ATOM C CA PRO A 113 . −6.162 7.498 13.130 1.00 23.25 . 1 838 ATOM C C PRO A 113 . −7.374 7.442 14.063 1.00 23.13 . 1 839 ATOM O O PRO A 113 . −7.820 8.472 14.617 1.00 22.81 . 1 840 ATOM C CB PRO A 113 . −6.557 7.806 11.667 1.00 22.31 . 1 841 ATOM C CG PRO A 113 . −5.495 7.218 10.906 1.00 22.92 . 1 842 ATOM C CD PRO A 113 . −5.300 5.842 11.599 1.00 23.93 . 1 843 HETA N N MSE A 114 . −7.927 6.239 14.233 1.00 24.20 . 1 844 HETA C CA MSE A 114 . −9.064 6.015 15.124 1.00 24.72 . 1 845 HETA C C MSE A 114 . −8.559 6.163 16.588 1.00 24.54 . 1 846 HETA O O MSE A 114 . −9.170 6.848 17.429 1.00 23.52 . 1 847 HETA C CB MSE A 114 . −9.594 4.594 14.846 1.00 27.78 . 1 848 HETA C CG MSE A 114 . −10.897 4.226 15.407 1.00 30.06 . 1 849 HETA SE SE MSE A 114 . −11.292 2.554 14.679 1.00 29.43 . 1 850 HETA C CE MSE A 114 . −12.286 2.884 13.126 1.00 34.13 . 1 851 ATOM N N VAL A 115 . −7.380 5.590 16.876 1.00 21.70 . 1 852 ATOM C CA VAL A 115 . −6.815 5.695 18.214 1.00 22.17 . 1 853 ATOM C C VAL A 115 . −6.659 7.187 18.562 1.00 21.32 . 1 854 ATOM O O VAL A 115 . −7.066 7.633 19.627 1.00 23.93 . 1 855 ATOM C CB VAL A 115 . −5.358 5.030 18.316 1.00 21.76 . 1 856 ATOM C CG1 VAL A 115 . −4.799 5.185 19.697 1.00 22.18 . 1 857 ATOM C CG2 VAL A 115 . −5.401 3.530 17.964 1.00 22.64 . 1 858 ATOM N N GLU A 116 . −6.104 7.963 17.645 1.00 22.38 . 1 859 ATOM C CA GLU A 116 . −5.862 9.377 17.936 1.00 22.76 . 1 860 ATOM C C GLU A 116 . −7.101 10.226 18.094 1.00 24.30 . 1 861 ATOM O O GLU A 116 . −7.162 11.133 18.952 1.00 24.18 . 1 862 ATOM C CB GLU A 116 . −4.936 9.973 16.888 1.00 24.96 . 1 863 ATOM C CG GLU A 116 . −3.585 9.300 16.954 1.00 25.68 . 1 864 ATOM C CD GLU A 116 . −2.497 10.104 16.289 1.00 28.70 . 1 865 ATOM O OE1 GLU A 116 . −2.388 10.043 15.047 1.00 27.97 . 1 866 ATOM O OE2 GLU A 116 . −1.755 10.831 17.027 1.00 30.94 . 1 867 ATOM N N CYS A 117 . −8.115 9.938 17.286 1.00 22.02 . 1 868 ATOM C CA CYS A 117 . −9.338 10.705 17.376 1.00 23.38 . 1 869 ATOM C C CYS A 117 . −10.089 10.397 18.660 1.00 22.58 . 1 870 ATOM O O CYS A 117 . −10.487 11.305 19.374 1.00 22.12 . 1 871 ATOM C CB CYS A 117 . −10.229 10.384 16.160 1.00 23.95 . 1 872 ATOM S SG CYS A 117 . −11.873 11.261 16.113 1.00 26.35 . 1 873 ATOM N N VAL A 118 . −10.337 9.122 18.910 1.00 20.11 . 1 874 ATOM C CA VAL A 118 . −11.085 8.680 20.053 1.00 20.90 . 1 875 ATOM C C VAL A 118 . −10.450 9.125 21.350 1.00 20.55 . 1 876 ATOM O O VAL A 118 . −11.149 9.514 22.300 1.00 21.04 . 1 877 ATOM C CB VAL A 118 . −11.228 7.119 20.052 1.00 20.25 . 1 878 ATOM C CG1 VAL A 118 . −11.939 6.637 21.307 1.00 21.86 . 1 879 ATOM C CG2 VAL A 118 . −12.017 6.686 18.796 1.00 22.14 . 1 880 ATOM N N LEU A 119 . −9.117 9.069 21.386 1.00 21.56 . 1 881 ATOM C CA LEU A 119 . −8.404 9.414 22.629 1.00 20.96 . 1 882 ATOM C C LEU A 119 . −7.968 10.865 22.742 1.00 22.41 . 1 883 ATOM O O LEU A 119 . −7.005 11.205 23.456 1.00 21.54 . 1 884 ATOM C CB LEU A 119 . −7.241 8.451 22.819 1.00 21.27 . 1 885 ATOM C CG LEU A 119 . −7.767 7.009 22.982 1.00 19.83 . 1 886 ATOM C CD1 LEU A 119 . −6.575 6.048 23.180 1.00 18.62 . 1 887 ATOM C CD2 LEU A 119 . −8.814 6.901 24.169 1.00 22.57 . 1 888 ATOM N N ASP A 120 . −8.622 11.724 21.980 1.00 20.94 . 1 889 ATOM C CA ASP A 120 . −8.396 13.175 22.106 1.00 21.40 . 1 890 ATOM C C ASP A 120 . −8.678 13.519 23.574 1.00 21.27 . 1 891 ATOM O O ASP A 120 . −9.614 12.991 24.144 1.00 22.40 . 1 892 ATOM C CB ASP A 120 . −9.386 13.922 21.255 1.00 22.71 . 1 893 ATOM C CG ASP A 120 . −9.258 15.427 21.409 1.00 22.78 . 1 894 ATOM O OD1 ASP A 120 . −10.064 15.986 22.163 1.00 23.91 . 1 895 ATOM O OD2 ASP A 120 . −8.361 16.028 20.766 1.00 27.26 . 1 896 ATOM N N PRO A 121 . −7.882 14.402 24.188 1.00 21.36 . 1 897 ATOM C CA PRO A 121 . −8.151 14.706 25.588 1.00 21.79 . 1 898 ATOM C C PRO A 121 . −9.550 15.238 25.892 1.00 22.28 . 1 899 ATOM O O PRO A 121 . −10.132 14.896 26.909 1.00 23.05 . 1 900 ATOM C CB PRO A 121 . −7.061 15.740 25.961 1.00 20.57 . 1 901 ATOM C CG PRO A 121 . −5.921 15.409 25.038 1.00 22.32 . 1 902 ATOM C CD PRO A 121 . −6.614 15.001 23.716 1.00 22.24 . 1 903 ATOM N N THR A 122 . −10.055 16.104 25.029 1.00 22.75 . 1 904 ATOM C CA THR A 122 . −11.357 16.715 25.245 1.00 24.10 . 1 905 ATOM C C THR A 122 . −12.504 15.764 25.028 1.00 24.02 . 1 906 ATOM O O THR A 122 . −13.454 15.690 25.844 1.00 24.28 . 1 907 ATOM C CB THR A 122 . −11.498 17.919 24.345 1.00 25.98 . 1 908 ATOM O OG1 THR A 122 . −10.391 18.787 24.612 1.00 27.56 . 1 909 ATOM C CG2 THR A 122 . −12.792 18.692 24.659 1.00 26.94 . 1 910 ATOM N N LEU A 123 . −12.391 14.996 23.958 1.00 23.90 . 1 911 ATOM C CA LEU A 123 . −13.437 14.020 23.644 1.00 22.68 . 1 912 ATOM C C LEU A 123 . −13.480 12.847 24.620 1.00 22.85 . 1 913 ATOM O O LEU A 123 . −14.551 12.543 25.179 1.00 22.31 . 1 914 ATOM C CB LEU A 123 . −13.288 13.518 22.189 1.00 24.07 . 1 915 ATOM C CG LEU A 123 . −13.296 14.549 21.036 1.00 26.21 . 1 916 ATOM C CD1 LEU A 123 . −13.202 13.824 19.710 1.00 27.12 . 1 917 ATOM C CD2 LEU A 123 . −14.564 15.373 21.083 1.00 26.58 . 1 918 ATOM N N SER A 124 . −12.331 12.225 24.874 1.00 21.46 . 1 919 ATOM C CA SER A 124 . −12.309 11.092 25.804 1.00 22.36 . 1 920 ATOM C C SER A 124 . −12.562 11.593 27.207 1.00 22.19 . 1 921 ATOM O O SER A 124 . −13.248 10.925 27.976 1.00 21.10 . 1 922 ATOM C CB SER A 124 . −10.991 10.301 25.706 1.00 22.55 . 1 923 ATOM O OG SER A 124 . −9.835 11.020 26.161 1.00 21.74 . 1 924 ATOM N N GLY A 125 . −12.049 12.790 27.500 1.00 21.47 . 1 925 ATOM C CA GLY A 125 . −12.265 13.390 28.820 1.00 22.36 . 1 926 ATOM C C GLY A 125 . −13.735 13.653 29.106 1.00 21.86 . 1 927 ATOM O O GLY A 125 . −14.138 13.751 30.267 1.00 20.85 . 1 928 ATOM N N SER A 126 . −14.523 13.771 28.047 1.00 19.69 . 1 929 ATOM C CA SER A 126 . −15.959 13.972 28.212 1.00 21.39 . 1 930 ATOM C C SER A 126 . −16.601 12.897 29.076 1.00 19.58 . 1 931 ATOM O O SER A 126 . −17.618 13.139 29.714 1.00 19.48 . 1 932 ATOM C CB SER A 126 . −16.656 13.983 26.841 1.00 21.87 . 1 933 ATOM O OG SER A 126 . −16.078 15.024 26.085 1.00 26.78 . 1 934 ATOM N N TYR A 127 . −16.009 11.699 29.123 1.00 20.00 . 1 935 ATOM C CA TYR A 127 . −16.609 10.607 29.880 1.00 20.16 . 1 936 ATOM C C TYR A 127 . −16.507 10.780 31.398 1.00 19.78 . 1 937 ATOM O O TYR A 127 . −17.015 9.967 32.156 1.00 21.09 . 1 938 ATOM C CB TYR A 127 . −16.060 9.255 29.389 1.00 19.40 . 1 939 ATOM C CG TYR A 127 . −16.553 8.939 27.961 1.00 21.03 . 1 940 ATOM C CD1 TYR A 127 . −16.014 9.596 26.883 1.00 21.94 . 1 941 ATOM C CD2 TYR A 127 . −17.629 8.050 27.733 1.00 20.86 . 1 942 ATOM C CE1 TYR A 127 . −16.487 9.409 25.606 1.00 21.15 . 1 943 ATOM C CE2 TYR A 127 . −18.135 7.867 26.448 1.00 18.74 . 1 944 ATOM C CZ TYR A 127 . −17.563 8.536 25.386 1.00 21.40 . 1 945 ATOM O OH TYR A 127 . −18.006 8.396 24.100 1.00 20.33 . 1 946 ATOM N N HIS A 128 . −15.808 11.831 31.826 1.00 19.22 . 1 947 ATOM C CA HIS A 128 . −15.778 12.153 33.263 1.00 19.24 . 1 948 ATOM C C HIS A 128 . −17.133 12.752 33.682 1.00 20.58 . 1 949 ATOM O O HIS A 128 . −17.427 12.828 34.896 1.00 22.07 . 1 950 ATOM C CB HIS A 128 . −14.715 13.202 33.590 1.00 19.89 . 1 951 ATOM C CG HIS A 128 . −13.335 12.667 33.672 1.00 20.50 . 1 952 ATOM N ND1 HIS A 128 . −12.863 11.968 34.769 1.00 21.47 . 1 953 ATOM C CD2 HIS A 128 . −12.316 12.704 32.784 1.00 20.71 . 1 954 ATOM C CE1 HIS A 128 . −11.617 11.609 34.556 1.00 20.31 . 1 955 ATOM N NE2 HIS A 128 . −11.261 12.030 33.358 1.00 19.60 . 1 956 ATOM N N GLU A 129 . −17.943 13.165 32.698 1.00 20.21 . 1 957 ATOM C CA GLU A 129 . −19.244 13.745 32.993 1.00 21.29 . 1 958 ATOM C C GLU A 129 . −20.458 12.844 32.751 1.00 19.84 . 1 959 ATOM O O GLU A 129 . −21.580 13.323 32.518 1.00 20.60 . 1 960 ATOM C CB GLU A 129 . −19.399 15.066 32.252 1.00 23.31 . 1 961 ATOM C CG GLU A 129 . −18.286 16.094 32.478 1.00 28.29 . 1 962 ATOM C CD GLU A 129 . −18.144 16.480 33.948 1.00 32.65 . 1 963 ATOM O OE1 GLU A 129 . −19.178 16.746 34.593 1.00 35.35 . 1 964 ATOM O OE2 GLU A 129 . −16.981 16.516 34.449 1.00 38.09 . 1 965 ATOM N N LEU A 130 . −20.245 11.542 32.797 1.00 19.70 . 1 966 ATOM C CA LEU A 130 . −21.383 10.630 32.661 1.00 20.41 . 1 967 ATOM C C LEU A 130 . −22.501 10.993 33.677 1.00 21.23 . 1 968 ATOM O O LEU A 130 . −23.685 10.950 33.322 1.00 21.71 . 1 969 ATOM C CB LEU A 130 . −20.933 9.180 32.887 1.00 21.17 . 1 970 ATOM C CG LEU A 130 . −20.146 8.608 31.703 1.00 19.70 . 1 971 ATOM C CD1 LEU A 130 . −19.666 7.161 32.073 1.00 18.04 . 1 972 ATOM C CD2 LEU A 130 . −21.062 8.555 30.429 1.00 21.60 . 1 973 ATOM N N LYS A 131 . −22.144 11.368 34.921 1.00 21.08 . 1 974 ATOM C CA LYS A 131 . −23.190 11.721 35.905 1.00 21.45 . 1 975 ATOM C C LYS A 131 . −23.987 12.944 35.417 1.00 21.63 . 1 976 ATOM O O LYS A 131 . −25.204 12.898 35.342 1.00 22.50 . 1 977 ATOM C CB LYS A 131 . −22.582 12.044 37.301 1.00 22.90 . 1 978 ATOM C CG LYS A 131 . −23.654 12.487 38.312 1.00 22.11 . 1 979 ATOM C CD LYS A 131 . −23.058 12.493 39.735 1.00 28.02 . 1 980 ATOM C CE LYS A 131 . −24.117 13.069 40.693 1.00 28.13 . 1 981 ATOM N NZ LYS A 131 . −23.619 12.979 42.118 1.00 31.26 . 1 982 ATOM N N LYS A 132 . −23.331 14.021 35.092 1.00 21.55 . 1 983 ATOM C CA LYS A 132 . −24.139 15.178 34.630 1.00 22.12 . 1 984 ATOM C C LYS A 132 . −25.030 14.785 33.441 1.00 21.54 . 1 985 ATOM O O LYS A 132 . −26.197 15.175 33.375 1.00 21.67 . 1 986 ATOM C CB LYS A 132 . −23.223 16.314 34.237 1.00 24.13 . 1 987 ATOM C CG LYS A 132 . −23.964 17.554 33.732 1.00 26.51 . 1 988 ATOM C CD LYS A 132 . −23.030 18.730 33.561 1.00 32.18 . 1 989 ATOM C CE LYS A 132 . −23.837 19.997 33.273 1.00 34.76 . 1 990 ATOM N NZ LYS A 132 . −23.009 21.167 32.912 1.00 35.94 . 1 991 ATOM N N TRP A 133 . −24.459 14.054 32.499 1.00 20.73 . 1 992 ATOM C CA TRP A 133 . −25.185 13.594 31.318 1.00 21.03 . 1 993 ATOM C C TRP A 133 . −26.387 12.722 31.617 1.00 21.39 . 1 994 ATOM O O TRP A 133 . −27.444 12.856 30.974 1.00 20.93 . 1 995 ATOM C CB TRP A 133 . −24.214 12.840 30.388 1.00 20.48 . 1 996 ATOM C CG TRP A 133 . −24.884 12.065 29.262 1.00 19.65 . 1 997 ATOM C CD1 TRP A 133 . −25.559 12.593 28.180 1.00 21.05 . 1 998 ATOM C CD2 TRP A 133 . −25.005 10.657 29.168 1.00 18.88 . 1 999 ATOM N NE1 TRP A 133 . −26.090 11.572 27.425 1.00 18.74 . 1 1000 ATOM C CE2 TRP A 133 . −25.759 10.373 28.003 1.00 19.57 . 1 1001 ATOM C CE3 TRP A 133 . −24.548 9.581 29.955 1.00 20.11 . 1 1002 ATOM C CZ2 TRP A 133 . −26.066 9.075 27.605 1.00 18.84 . 1 1003 ATOM C CZ3 TRP A 133 . −24.854 8.296 29.556 1.00 18.37 . 1 1004 ATOM C CH2 TRP A 133 . −25.602 8.049 28.390 1.00 21.15 . 1 1005 ATOM N N ILE A 134 . −26.275 11.806 32.584 1.00 20.17 . 1 1006 ATOM C CA ILE A 134 . −27.391 10.919 32.853 1.00 21.33 . 1 1007 ATOM C C ILE A 134 . −28.594 11.686 33.427 1.00 21.56 . 1 1008 ATOM O O ILE A 134 . −29.725 11.204 33.384 1.00 22.40 . 1 1009 ATOM C CB ILE A 134 . −26.943 9.750 33.790 1.00 21.70 . 1 1010 ATOM C CG1 ILE A 134 . −27.841 8.535 33.554 1.00 24.84 . 1 1011 ATOM C CG2 ILE A 134 . −27.004 10.212 35.260 1.00 25.19 . 1 1012 ATOM C CD1 ILE A 134 . −27.444 7.700 32.358 1.00 25.79 . 1 1013 ATOM N N TYR A 135 . −28.338 12.896 33.932 1.00 22.23 . 1 1014 ATOM C CA TYR A 135 . −29.402 13.712 34.456 1.00 23.24 . 1 1015 ATOM C C TYR A 135 . −29.988 14.663 33.417 1.00 25.54 . 1 1016 ATOM O O TYR A 135 . −30.986 15.355 33.697 1.00 26.00 . 1 1017 ATOM C CB TYR A 135 . −28.928 14.462 35.715 1.00 23.38 . 1 1018 ATOM C CG TYR A 135 . −28.993 13.559 36.933 1.00 23.66 . 1 1019 ATOM C CD1 TYR A 135 . −27.832 13.089 37.519 1.00 24.15 . 1 1020 ATOM C CD2 TYR A 135 . −30.219 13.144 37.451 1.00 25.12 . 1 1021 ATOM C CE1 TYR A 135 . −27.878 12.216 38.605 1.00 24.38 . 1 1022 ATOM C CE2 TYR A 135 . −30.297 12.258 38.513 1.00 25.20 . 1 1023 ATOM C CZ TYR A 135 . −29.112 11.793 39.081 1.00 25.89 . 1 1024 ATOM O OH TYR A 135 . −29.157 10.854 40.095 1.00 27.00 . 1 1025 ATOM N N GLU A 136 . −29.395 14.692 32.217 1.00 23.59 . 1 1026 ATOM C CA GLU A 136 . −29.907 15.586 31.170 1.00 25.41 . 1 1027 ATOM C C GLU A 136 . −31.030 14.918 30.387 1.00 25.71 . 1 1028 ATOM O O GLU A 136 . −30.848 13.849 29.828 1.00 24.28 . 1 1029 ATOM C CB GLU A 136 . −28.788 15.989 30.204 1.00 25.65 . 1 1030 ATOM C CG GLU A 136 . −27.732 16.896 30.791 1.00 28.04 . 1 1031 ATOM C CD GLU A 136 . −28.297 18.289 31.117 1.00 30.46 . 1 1032 ATOM O OE1 GLU A 136 . −29.328 18.715 30.491 1.00 27.12 . 1 1033 ATOM O OE2 GLU A 136 . −27.702 18.956 32.006 1.00 30.71 . 1 1034 ATOM N N GLU A 137 . −32.198 15.561 30.310 1.00 27.37 . 1 1035 ATOM C CA GLU A 137 . −33.320 14.979 29.574 1.00 29.69 . 1 1036 ATOM C C GLU A 137 . −33.037 14.764 28.091 1.00 30.27 . 1 1037 ATOM O O GLU A 137 . −33.453 13.745 27.521 1.00 30.18 . 1 1038 ATOM C CB GLU A 137 . −34.525 15.909 29.602 1.00 33.38 . 1 1039 ATOM C CG GLU A 137 . −35.207 16.134 30.914 1.00 39.20 . 1 1040 ATOM C CD GLU A 137 . −36.313 17.192 30.763 1.00 43.90 . 1 1041 ATOM O OE1 GLU A 137 . −37.140 17.030 29.835 1.00 45.40 . 1 1042 ATOM O OE2 GLU A 137 . −36.359 18.176 31.558 1.00 46.36 . 1 1043 ATOM N N ASP A 138 . −32.371 15.762 27.492 1.00 28.25 . 1 1044 ATOM C CA ASP A 138 . −32.044 15.833 26.064 1.00 28.52 . 1 1045 ATOM C C ASP A 138 . −30.586 15.778 25.620 1.00 27.60 . 1 1046 ATOM O O ASP A 138 . −30.251 15.214 24.554 1.00 27.81 . 1 1047 ATOM C CB ASP A 138 . −32.560 17.147 25.478 1.00 31.84 . 1 1048 ATOM C CG ASP A 138 . −34.046 17.330 25.679 1.00 34.48 . 1 1049 ATOM O OD1 ASP A 138 . −34.794 16.351 25.493 1.00 36.44 . 1 1050 ATOM O OD2 ASP A 138 . −34.456 18.470 26.003 1.00 38.65 . 1 1051 ATOM N N LEU A 139 . −29.718 16.421 26.370 1.00 25.84 . 1 1052 ATOM C CA LEU A 139 . −28.341 16.466 25.923 1.00 24.45 . 1 1053 ATOM C C LEU A 139 . −27.645 15.143 25.761 1.00 21.95 . 1 1054 ATOM O O LEU A 139 . −27.881 14.177 26.511 1.00 22.25 . 1 1055 ATOM C CB LEU A 139 . −27.465 17.355 26.832 1.00 26.30 . 1 1056 ATOM C CG LEU A 139 . −27.840 18.849 26.824 1.00 26.62 . 1 1057 ATOM C CD1 LEU A 139 . −26.860 19.642 27.708 1.00 28.85 . 1 1058 ATOM C CD2 LEU A 139 . −27.760 19.366 25.406 1.00 30.88 . 1 1059 ATOM N N THR A 140 . −26.787 15.144 24.755 1.00 23.40 . 1 1060 ATOM C CA THR A 140 . −25.864 14.020 24.471 1.00 22.73 . 1 1061 ATOM C C THR A 140 . −24.651 14.266 25.384 1.00 23.28 . 1 1062 ATOM O O THR A 140 . −24.424 15.398 25.867 1.00 23.27 . 1 1063 ATOM C CB THR A 140 . −25.345 14.048 23.009 1.00 23.35 . 1 1064 ATOM O OG1 THR A 140 . −24.611 15.272 22.752 1.00 23.69 . 1 1065 ATOM C CG2 THR A 140 . −26.529 13.952 22.072 1.00 25.79 . 1 1066 ATOM N N LEU A 141 . −23.867 13.221 25.636 1.00 22.02 . 1 1067 ATOM C CA LEU A 141 . −22.667 13.425 26.467 1.00 22.97 . 1 1068 ATOM C C LEU A 141 . −21.735 14.489 25.852 1.00 23.23 . 1 1069 ATOM O O LEU A 141 . −21.225 15.351 26.571 1.00 23.19 . 1 1070 ATOM C CB LEU A 141 . −21.918 12.103 26.662 1.00 22.75 . 1 1071 ATOM C CG LEU A 141 . −20.608 12.213 27.459 1.00 22.81 . 1 1072 ATOM C CD1 LEU A 141 . −20.946 12.558 28.940 1.00 20.39 . 1 1073 ATOM C CD2 LEU A 141 . −19.852 10.939 27.404 1.00 26.13 . 1 1074 ATOM N N PHE A 142 . −21.461 14.433 24.547 1.00 22.26 . 1 1075 ATOM C CA PHE A 142 . −20.623 15.475 23.974 1.00 24.85 . 1 1076 ATOM C C PHE A 142 . −21.335 16.835 24.050 1.00 24.91 . 1 1077 ATOM O O PHE A 142 . −20.668 17.861 24.119 1.00 27.99 . 1 1078 ATOM C CB PHE A 142 . −20.246 15.191 22.516 1.00 24.86 . 1 1079 ATOM C CG PHE A 142 . −19.158 14.187 22.342 1.00 24.09 . 1 1080 ATOM C CD1 PHE A 142 . −18.860 13.715 21.059 1.00 24.01 . 1 1081 ATOM C CD2 PHE A 142 . −18.389 13.712 23.419 1.00 26.49 . 1 1082 ATOM C CE1 PHE A 142 . −17.828 12.790 20.824 1.00 24.76 . 1 1083 ATOM C CE2 PHE A 142 . −17.339 12.769 23.194 1.00 24.44 . 1 1084 ATOM C CZ PHE A 142 . −17.068 12.317 21.900 1.00 24.27 . 1 1085 ATOM N N GLY A 143 . −22.664 16.860 24.022 1.00 23.97 . 1 1086 ATOM C CA GLY A 143 . −23.382 18.137 24.092 1.00 25.52 . 1 1087 ATOM C C GLY A 143 . −23.182 18.818 25.446 1.00 27.41 . 1 1088 ATOM O O GLY A 143 . −23.217 20.072 25.568 1.00 28.69 . 1 1089 ATOM N N VAL A 144 . −22.989 17.995 26.466 1.00 27.06 . 1 1090 ATOM C CA VAL A 144 . −22.728 18.466 27.838 1.00 27.07 . 1 1091 ATOM C C VAL A 144 . −21.345 19.116 27.968 1.00 28.28 . 1 1092 ATOM O O VAL A 144 . −21.173 20.193 28.584 1.00 28.66 . 1 1093 ATOM C CB VAL A 144 . −22.810 17.265 28.849 1.00 27.33 . 1 1094 ATOM C CG1 VAL A 144 . −22.233 17.657 30.219 1.00 27.12 . 1 1095 ATOM C CG2 VAL A 144 . −24.232 16.872 29.024 1.00 27.69 . 1 1096 ATOM N N THR A 145 . −20.358 18.458 27.384 1.00 25.60 . 1 1097 ATOM C CA THR A 145 . −18.981 18.870 27.475 1.00 26.35 . 1 1098 ATOM C C THR A 145 . −18.440 19.857 26.450 1.00 26.97 . 1 1099 ATOM O O THR A 145 . −17.549 20.643 26.767 1.00 26.63 . 1 1100 ATOM C CB THR A 145 . −18.126 17.610 27.505 1.00 26.02 . 1 1101 ATOM O OG1 THR A 145 . −18.199 16.986 26.211 1.00 26.09 . 1 1102 ATOM C CG2 THR A 145 . −18.721 16.618 28.524 1.00 27.22 . 1 1103 ATOM N N LEU A 146 . −18.980 19.854 25.233 1.00 26.85 . 1 1104 ATOM C CA LEU A 146 . −18.437 20.728 24.191 1.00 27.85 . 1 1105 ATOM C C LEU A 146 . −19.181 22.035 24.051 1.00 28.87 . 1 1106 ATOM O O LEU A 146 . −18.715 22.937 23.350 1.00 31.43 . 1 1107 ATOM C CB LEU A 146 . −18.408 20.009 22.823 1.00 26.31 . 1 1108 ATOM C CG LEU A 146 . −17.752 18.620 22.771 1.00 25.20 . 1 1109 ATOM C CD1 LEU A 146 . −17.967 17.989 21.412 1.00 27.35 . 1 1110 ATOM C CD2 LEU A 146 . −16.250 18.739 23.019 1.00 26.88 . 1 1111 ATOM N N GLY A 147 . −20.342 22.133 24.682 1.00 29.99 . 1 1112 ATOM C CA GLY A 147 . −21.113 23.373 24.611 1.00 31.11 . 1 1113 ATOM C C GLY A 147 . −21.864 23.607 23.310 1.00 32.46 . 1 1114 ATOM O O GLY A 147 . −22.282 24.750 23.025 1.00 33.30 . 1 1115 ATOM N N SER A 148 . −22.007 22.548 22.509 1.00 30.19 . 1 1116 ATOM C CA SER A 148 . −22.771 22.590 21.248 1.00 30.16 . 1 1117 ATOM C C SER A 148 . −22.884 21.147 20.809 1.00 29.82 . 1 1118 ATOM O O SER A 148 . −22.210 20.266 21.394 1.00 29.75 . 1 1119 ATOM C CB SER A 148 . −22.057 23.413 20.148 1.00 30.15 . 1 1120 ATOM O OG SER A 148 . −20.970 22.732 19.539 1.00 30.17 . 1 1121 ATOM N N GLY A 149 . −23.762 20.909 19.819 1.00 28.01 . 1 1122 ATOM C CA GLY A 149 . −23.918 19.574 19.265 1.00 28.10 . 1 1123 ATOM C C GLY A 149 . −22.608 19.224 18.595 1.00 27.14 . 1 1124 ATOM O O GLY A 149 . −21.826 20.104 18.150 1.00 26.79 . 1 1125 ATOM N N PHE A 150 . −22.356 17.926 18.499 1.00 25.93 . 1 1126 ATOM C CA PHE A 150 . −21.108 17.456 17.910 1.00 24.91 . 1 1127 ATOM C C PHE A 150 . −20.898 17.890 16.466 1.00 25.50 . 1 1128 ATOM O O PHE A 150 . −19.808 18.265 16.107 1.00 24.02 . 1 1129 ATOM C CB PHE A 150 . −21.057 15.911 18.010 1.00 23.38 . 1 1130 ATOM C CG PHE A 150 . −19.774 15.287 17.488 1.00 24.27 . 1 1131 ATOM C CD1 PHE A 150 . −18.563 15.510 18.149 1.00 21.98 . 1 1132 ATOM C CD2 PHE A 150 . −19.781 14.477 16.321 1.00 22.53 . 1 1133 ATOM C CE1 PHE A 150 . −17.398 14.967 17.698 1.00 23.28 . 1 1134 ATOM C CE2 PHE A 150 . −18.600 13.909 15.845 1.00 22.13 . 1 1135 ATOM C CZ PHE A 150 . −17.389 14.153 16.542 1.00 23.90 . 1 1136 ATOM N N TRP A 151 . −21.929 17.808 15.629 1.00 24.40 . 1 1137 ATOM C CA TRP A 151 . −21.720 18.187 14.231 1.00 24.88 . 1 1138 ATOM C C TRP A 151 . −21.424 19.670 14.080 1.00 25.97 . 1 1139 ATOM O O TRP A 151 . −20.616 20.051 13.258 1.00 27.64 . 1 1140 ATOM C CB TRP A 151 . −22.920 17.747 13.398 1.00 24.08 . 1 1141 ATOM C CG TRP A 151 . −23.190 16.275 13.591 1.00 23.74 . 1 1142 ATOM C CD1 TRP A 151 . −24.296 15.712 14.167 1.00 21.76 . 1 1143 ATOM C CD2 TRP A 151 . −22.279 15.181 13.325 1.00 22.94 . 1 1144 ATOM N NE1 TRP A 151 . −24.130 14.343 14.273 1.00 21.21 . 1 1145 ATOM C CE2 TRP A 151 . −22.901 14.001 13.773 1.00 24.05 . 1 1146 ATOM C CE3 TRP A 151 . −20.995 15.095 12.761 1.00 26.23 . 1 1147 ATOM C CZ2 TRP A 151 . −22.269 12.725 13.675 1.00 20.74 . 1 1148 ATOM C CZ3 TRP A 151 . −20.372 13.854 12.655 1.00 24.61 . 1 1149 ATOM C CH2 TRP A 151 . −21.005 12.683 13.111 1.00 24.99 . 1 1150 ATOM N N ASP A 152 . −22.057 20.519 14.886 1.00 27.91 . 1 1151 ATOM C CA ASP A 152 . −21.762 21.916 14.837 1.00 29.10 . 1 1152 ATOM C C ASP A 152 . −20.368 22.210 15.349 1.00 29.04 . 1 1153 ATOM O O ASP A 152 . −19.660 23.082 14.860 1.00 29.22 . 1 1154 ATOM C CB ASP A 152 . −22.841 22.622 15.646 1.00 31.64 . 1 1155 ATOM C CG ASP A 152 . −24.214 22.363 15.042 1.00 36.99 . 1 1156 ATOM O OD1 ASP A 152 . −24.272 22.000 13.846 1.00 20.03 . 1 1157 ATOM O OD2 ASP A 152 . −25.225 22.510 15.758 1.00 20.03 . 1 1158 ATOM N N PHE A 153 . −19.957 21.457 16.382 1.00 26.82 . 1 1159 ATOM C CA PHE A 153 . −18.621 21.577 16.930 1.00 27.26 . 1 1160 ATOM C C PHE A 153 . −17.564 21.263 15.843 1.00 26.02 . 1 1161 ATOM O O PHE A 153 . −16.539 21.933 15.731 1.00 27.56 . 1 1162 ATOM C CB PHE A 153 . −18.497 20.607 18.133 1.00 26.63 . 1 1163 ATOM C CG PHE A 153 . −17.109 20.484 18.699 1.00 29.20 . 1 1164 ATOM C CD1 PHE A 153 . −16.602 21.417 19.617 1.00 29.27 . 1 1165 ATOM C CD2 PHE A 153 . −16.310 19.415 18.321 1.00 29.84 . 1 1166 ATOM C CE1 PHE A 153 . −15.332 21.271 20.139 1.00 31.77 . 1 1167 ATOM C CE2 PHE A 153 . −15.014 19.257 18.851 1.00 31.81 . 1 1168 ATOM C CZ PHE A 153 . −14.539 20.187 19.759 1.00 33.05 . 1 1169 ATOM N N LEU A 154 . −17.792 20.232 15.032 1.00 25.77 . 1 1170 ATOM C CA LEU A 154 . −16.837 19.900 14.007 1.00 25.32 . 1 1171 ATOM C C LEU A 154 . −16.764 21.043 13.014 1.00 26.21 . 1 1172 ATOM O O LEU A 154 . −15.710 21.316 12.459 1.00 26.62 . 1 1173 ATOM C CB LEU A 154 . −17.258 18.628 13.297 1.00 25.79 . 1 1174 ATOM C CG LEU A 154 . −17.050 17.353 14.112 1.00 24.47 . 1 1175 ATOM C CD1 LEU A 154 . −17.284 16.184 13.156 1.00 21.99 . 1 1176 ATOM C CD2 LEU A 154 . −15.630 17.267 14.759 1.00 23.22 . 1 1177 ATOM N N ASP A 155 . −17.900 21.719 12.822 1.00 26.34 . 1 1178 ATOM C CA ASP A 155 . −17.951 22.824 11.838 1.00 28.67 . 1 1179 ATOM C C ASP A 155 . −17.131 24.020 12.304 1.00 29.53 . 1 1180 ATOM O O ASP A 155 . −16.679 24.834 11.486 1.00 31.16 . 1 1181 ATOM C CB ASP A 155 . −19.393 23.276 11.630 1.00 27.84 . 1 1182 ATOM C CG ASP A 155 . −20.184 22.379 10.683 1.00 29.44 . 1 1183 ATOM O OD1 ASP A 155 . −19.635 21.451 10.019 1.00 28.74 . 1 1184 ATOM O OD2 ASP A 155 . −21.414 22.612 10.578 1.00 31.69 . 1 1185 ATOM N N LYS A 156 . −16.949 24.141 13.613 1.00 30.26 . 1 1186 ATOM C CA LYS A 156 . −16.205 25.265 14.197 1.00 31.03 . 1 1187 ATOM C C LYS A 156 . −14.732 24.927 14.556 1.00 31.50 . 1 1188 ATOM O O LYS A 156 . −13.919 25.824 14.892 1.00 31.72 . 1 1189 ATOM C CB LYS A 156 . −16.950 25.744 15.450 1.00 32.82 . 1 1190 ATOM C CG LYS A 156 . −18.237 26.524 15.160 1.00 34.11 . 1 1191 ATOM C CD LYS A 156 . −18.873 27.020 16.459 1.00 37.81 . 1 1192 ATOM C CE LYS A 156 . −19.869 28.159 16.192 1.00 40.87 . 1 1193 ATOM N NZ LYS A 156 . −20.279 28.826 17.465 1.00 42.81 . 1 1194 ATOM N N ASN A 157 . −14.367 23.646 14.484 1.00 28.10 . 1 1195 ATOM C CA ASN A 157 . −13.030 23.250 14.876 1.00 27.75 . 1 1196 ATOM C C ASN A 157 . −12.397 22.394 13.798 1.00 28.05 . 1 1197 ATOM O O ASN A 157 . −12.517 21.155 13.812 1.00 26.85 . 1 1198 ATOM C CB ASN A 157 . −13.147 22.504 16.209 1.00 26.92 . 1 1199 ATOM C CG ASN A 157 . −13.623 23.428 17.347 1.00 27.86 . 1 1200 ATOM O OD1 ASN A 157 . −12.803 24.132 17.961 1.00 29.00 . 1 1201 ATOM N ND2 ASN A 157 . −14.945 23.448 17.618 1.00 28.01 . 1 1202 ATOM N N PRO A 158 . −11.762 23.031 12.808 1.00 28.79 . 1 1203 ATOM C CA PRO A 158 . −11.105 22.367 11.681 1.00 29.44 . 1 1204 ATOM C C PRO A 158 . −10.211 21.176 12.018 1.00 29.93 . 1 1205 ATOM O O PRO A 158 . −10.273 20.148 11.346 1.00 31.40 . 1 1206 ATOM C CB PRO A 158 . −10.317 23.511 11.012 1.00 30.34 . 1 1207 ATOM C CG PRO A 158 . −11.145 24.653 11.281 1.00 30.26 . 1 1208 ATOM C CD PRO A 158 . −11.534 24.490 12.734 1.00 28.30 . 1 1209 ATOM N N GLU A 159 . −9.346 21.313 13.016 1.00 30.02 . 1 1210 ATOM C CA GLU A 159 . −8.490 20.188 13.371 1.00 30.58 . 1 1211 ATOM C C GLU A 159 . −9.301 18.977 13.860 1.00 28.51 . 1 1212 ATOM O O GLU A 159 . −8.875 17.843 13.618 1.00 29.58 . 1 1213 ATOM C CB GLU A 159 . −7.481 20.624 14.424 1.00 32.96 . 1 1214 ATOM C CG GLU A 159 . −6.851 21.931 14.011 1.00 38.77 . 1 1215 ATOM C CD GLU A 159 . −5.986 22.516 15.094 1.00 41.78 . 1 1216 ATOM O OE1 GLU A 159 . −5.044 21.805 15.517 1.00 43.02 . 1 1217 ATOM O OE2 GLU A 159 . −6.256 23.682 15.509 1.00 44.62 . 1 1218 ATOM N N TYR A 160 . −10.426 19.209 14.543 1.00 26.41 . 1 1219 ATOM C CA TYR A 160 . −11.252 18.100 15.024 1.00 26.76 . 1 1220 ATOM C C TYR A 160 . −11.995 17.476 13.863 1.00 26.01 . 1 1221 ATOM O O TYR A 160 . −12.162 16.267 13.789 1.00 25.84 . 1 1222 ATOM C CB TYR A 160 . −12.282 18.530 16.078 1.00 26.30 . 1 1223 ATOM C CG TYR A 160 . −11.746 18.605 17.501 1.00 28.13 . 1 1224 ATOM C CD1 TYR A 160 . −11.157 19.776 18.006 1.00 29.01 . 1 1225 ATOM C CD2 TYR A 160 . −11.810 17.489 18.339 1.00 29.15 . 1 1226 ATOM C CE1 TYR A 160 . −10.643 19.818 19.329 1.00 28.84 . 1 1227 ATOM C CE2 TYR A 160 . −11.312 17.526 19.631 1.00 29.60 . 1 1228 ATOM C CZ TYR A 160 . −10.734 18.675 20.127 1.00 29.31 . 1 1229 ATOM O OH TYR A 160 . −10.278 18.666 21.442 1.00 30.09 . 1 1230 ATOM N N ASN A 161 . −12.450 18.327 12.965 1.00 26.00 . 1 1231 ATOM C CA ASN A 161 . −13.161 17.863 11.789 1.00 25.17 . 1 1232 ATOM C C ASN A 161 . −12.220 16.925 11.027 1.00 25.89 . 1 1233 ATOM O O ASN A 161 . −12.627 15.823 10.615 1.00 25.65 . 1 1234 ATOM C CB ASN A 161 . −13.551 19.059 10.905 1.00 26.45 . 1 1235 ATOM C CG ASN A 161 . −14.435 18.646 9.737 1.00 27.49 . 1 1236 ATOM O OD1 ASN A 161 . −14.038 18.747 8.549 1.00 30.02 . 1 1237 ATOM N ND2 ASN A 161 . −15.632 18.158 10.052 1.00 25.62 . 1 1238 ATOM N N THR A 162 . −10.961 17.333 10.854 1.00 27.77 . 1 1239 ATOM C CA THR A 162 . −9.971 16.525 10.145 1.00 26.94 . 1 1240 ATOM C C THR A 162 . −9.674 15.228 10.868 1.00 25.80 . 1 1241 ATOM O O THR A 162 . −9.650 14.166 10.255 1.00 26.58 . 1 1242 ATOM C CB THR A 162 . −8.676 17.311 9.922 1.00 28.80 . 1 1243 ATOM O OG1 THR A 162 . −8.987 18.431 9.080 1.00 28.76 . 1 1244 ATOM C CG2 THR A 162 . −7.627 16.440 9.197 1.00 29.19 . 1 1245 ATOM N N SER A 163 . −9.487 15.316 12.182 1.00 24.88 . 1 1246 ATOM C CA SER A 163 . −9.233 14.131 13.003 1.00 24.35 . 1 1247 ATOM C C SER A 163 . −10.394 13.119 12.814 1.00 24.24 . 1 1248 ATOM O O SER A 163 . −10.197 11.888 12.622 1.00 23.98 . 1 1249 ATOM C CB SER A 163 . −9.151 14.593 14.444 1.00 26.31 . 1 1250 ATOM O OG SER A 163 . −8.980 13.518 15.337 1.00 31.86 . 1 1251 ATOM N N PHE A 164 . −11.610 13.638 12.896 1.00 22.98 . 1 1252 ATOM C CA PHE A 164 . −12.819 12.803 12.745 1.00 22.57 . 1 1253 ATOM C C PHE A 164 . −12.837 12.178 11.344 1.00 24.40 . 1 1254 ATOM O O PHE A 164 . −13.044 10.972 11.220 1.00 23.70 . 1 1255 ATOM C CB PHE A 164 . −14.075 13.630 12.951 1.00 23.77 . 1 1256 ATOM C CG PHE A 164 . −15.342 12.842 12.762 1.00 24.03 . 1 1257 ATOM C CD1 PHE A 164 . −15.804 11.999 13.766 1.00 25.32 . 1 1258 ATOM C CD2 PHE A 164 . −16.065 12.949 11.568 1.00 27.62 . 1 1259 ATOM C CE1 PHE A 164 . −16.966 11.275 13.591 1.00 27.22 . 1 1260 ATOM C CE2 PHE A 164 . −17.241 12.217 11.379 1.00 24.78 . 1 1261 ATOM C CZ PHE A 164 . −17.685 11.399 12.367 1.00 26.44 . 1 1262 ATOM N N ASN A 165 . −12.632 12.986 10.295 1.00 25.03 . 1 1263 ATOM C CA ASN A 165 . −12.620 12.428 8.933 1.00 25.92 . 1 1264 ATOM C C ASN A 165 . −11.591 11.337 8.719 1.00 25.77 . 1 1265 ATOM O O ASN A 165 . −11.895 10.354 8.036 1.00 26.90 . 1 1266 ATOM C CB ASN A 165 . −12.376 13.507 7.882 1.00 27.12 . 1 1267 ATOM C CG ASN A 165 . −13.533 14.464 7.759 1.00 29.36 . 1 1268 ATOM O OD1 ASN A 165 . −14.683 14.131 8.084 1.00 31.06 . 1 1269 ATOM N ND2 ASN A 165 . −13.242 15.668 7.245 1.00 30.80 . 1 1270 ATOM N N ASP A 166 . −10.380 11.503 9.269 1.00 25.27 . 1 1271 ATOM C CA ASP A 166 . −9.361 10.487 9.154 1.00 25.36 . 1 1272 ATOM C C ASP A 166 . −9.747 9.224 9.928 1.00 25.65 . 1 1273 ATOM O O ASP A 166 . −9.429 8.103 9.498 1.00 24.49 . 1 1274 ATOM C CB ASP A 166 . −7.982 10.971 9.662 1.00 26.72 . 1 1275 ATOM C CG ASP A 166 . −7.400 12.132 8.847 1.00 29.64 . 1 1276 ATOM O OD1 ASP A 166 . −7.815 12.347 7.693 1.00 32.92 . 1 1277 ATOM O OD2 ASP A 166 . −6.512 12.823 9.371 1.00 30.94 . 1 1278 ATOM N N ALA A 167 . −10.430 9.383 11.056 1.00 23.83 . 1 1279 ATOM C CA ALA A 167 . −10.838 8.211 11.791 1.00 24.36 . 1 1280 ATOM C C ALA A 167 . −11.885 7.440 10.978 1.00 24.36 . 1 1281 ATOM O O ALA A 167 . −11.823 6.192 10.877 1.00 26.11 . 1 1282 ATOM C CB ALA A 167 . −11.378 8.609 13.171 1.00 24.28 . 1 1283 HETA N N MSE A 168 . −12.847 8.156 10.391 1.00 23.65 . 1 1284 HETA C CA MSE A 168 . −13.874 7.505 9.588 1.00 25.00 . 1 1285 HETA C C MSE A 168 . −13.281 6.810 8.360 1.00 24.01 . 1 1286 HETA O O MSE A 168 . −13.764 5.738 7.945 1.00 24.90 . 1 1287 HETA C CB MSE A 168 . −14.939 8.524 9.136 1.00 23.30 . 1 1288 HETA C CG MSE A 168 . −15.754 9.148 10.286 1.00 27.23 . 1 1289 HETA SE SE MSE A 168 . −16.709 7.929 11.350 1.00 24.13 . 1 1290 HETA C CE MSE A 168 . −17.390 6.969 10.067 1.00 24.98 . 1 1291 ATOM N N ALA A 169 . −12.221 7.395 7.807 1.00 23.26 . 1 1292 ATOM C CA ALA A 169 . −11.567 6.875 6.618 1.00 24.24 . 1 1293 ATOM C C ALA A 169 . −10.779 5.638 6.912 1.00 24.28 . 1 1294 ATOM O O ALA A 169 . −10.536 4.841 6.012 1.00 26.74 . 1 1295 ATOM C CB ALA A 169 . −10.623 7.893 6.056 1.00 25.84 . 1 1296 ATOM N N SER A 170 . −10.385 5.487 8.164 1.00 23.91 . 1 1297 ATOM C CA SER A 170 . −9.513 4.377 8.540 1.00 24.24 . 1 1298 ATOM C C SER A 170 . −10.016 2.980 8.231 1.00 25.28 . 1 1299 ATOM O O SER A 170 . −9.225 2.131 7.828 1.00 26.61 . 1 1300 ATOM C CB SER A 170 . −9.110 4.508 10.022 1.00 25.80 . 1 1301 ATOM O OG SER A 170 . −10.272 4.339 10.804 1.00 30.67 . 1 1302 ATOM N N ASP A 171 . −11.314 2.703 8.374 1.00 26.46 . 1 1303 ATOM C CA ASP A 171 . −11.782 1.342 7.998 1.00 26.72 . 1 1304 ATOM C C ASP A 171 . −12.696 1.415 6.764 1.00 28.07 . 1 1305 ATOM O O ASP A 171 . −13.370 0.439 6.419 1.00 27.47 . 1 1306 ATOM C CB ASP A 171 . −12.525 0.648 9.145 1.00 28.23 . 1 1307 ATOM C CG ASP A 171 . −13.801 1.347 9.555 1.00 28.00 . 1 1308 ATOM O OD1 ASP A 171 . −14.078 2.493 9.086 1.00 25.62 . 1 1309 ATOM O OD2 ASP A 171 . −14.506 0.740 10.413 1.00 27.50 . 1 1310 ATOM N N SER A 172 . −12.681 2.551 6.079 1.00 27.20 . 1 1311 ATOM C CA SER A 172 . −13.559 2.743 4.930 1.00 28.03 . 1 1312 ATOM C C SER A 172 . −13.269 1.827 3.764 1.00 28.87 . 1 1313 ATOM O O SER A 172 . −14.208 1.329 3.160 1.00 29.83 . 1 1314 ATOM C CB SER A 172 . −13.524 4.184 4.391 1.00 26.98 . 1 1315 ATOM O OG SER A 172 . −12.258 4.560 3.878 1.00 28.43 . 1 1316 ATOM N N LYS A 173 . −11.981 1.639 3.426 1.00 29.48 . 1 1317 ATOM C CA LYS A 173 . −11.635 0.756 2.299 1.00 31.00 . 1 1318 ATOM C C LYS A 173 . −12.269 −0.623 2.442 1.00 30.43 . 1 1319 ATOM O O LYS A 173 . −12.924 −1.106 1.523 1.00 29.58 . 1 1320 ATOM C CB LYS A 173 . −10.105 0.625 2.159 1.00 32.47 . 1 1321 ATOM C CG LYS A 173 . −9.420 1.973 1.875 1.00 38.04 . 1 1322 ATOM C CD LYS A 173 . −8.081 1.858 1.104 1.00 40.24 . 1 1323 ATOM C CE LYS A 173 . −7.555 3.263 0.761 1.00 41.94 . 1 1324 ATOM N NZ LYS A 173 . −6.234 3.262 0.051 1.00 43.94 . 1 1325 ATOM N N LEU A 174 . −12.114 −1.235 3.617 1.00 29.29 . 1 1326 ATOM C CA LEU A 174 . −12.661 −2.565 3.878 1.00 29.26 . 1 1327 ATOM C C LEU A 174 . −14.177 −2.639 3.753 1.00 29.62 . 1 1328 ATOM O O LEU A 174 . −14.757 −3.574 3.153 1.00 28.33 . 1 1329 ATOM C CB LEU A 174 . −12.311 −3.011 5.285 1.00 30.60 . 1 1330 ATOM C CG LEU A 174 . −11.469 −4.265 5.538 1.00 32.10 . 1 1331 ATOM C CD1 LEU A 174 . −11.625 −4.592 6.985 1.00 30.50 . 1 1332 ATOM C CD2 LEU A 174 . −11.884 −5.438 4.662 1.00 32.44 . 1 1333 ATOM N N ILE A 175 . −14.825 −1.633 4.311 1.00 26.91 . 1 1334 ATOM C CA ILE A 175 . −16.267 −1.656 4.295 1.00 25.44 . 1 1335 ATOM C C ILE A 175 . −16.793 −1.339 2.938 1.00 23.51 . 1 1336 ATOM O O ILE A 175 . −17.776 −1.976 2.505 1.00 22.43 . 1 1337 ATOM C CB ILE A 175 . −16.879 −0.632 5.258 1.00 23.18 . 1 1338 ATOM C CG1 ILE A 175 . −16.266 −0.830 6.646 1.00 24.69 . 1 1339 ATOM C CG2 ILE A 175 . −18.444 −0.766 5.272 1.00 21.19 . 1 1340 ATOM C CD1 ILE A 175 . −16.586 0.308 7.574 1.00 25.10 . 1 1341 ATOM N N ASN A 176 . −16.216 −0.332 2.287 1.00 22.91 . 1 1342 ATOM C CA ASN A 176 . −16.745 0.051 1.006 1.00 22.95 . 1 1343 ATOM C C ASN A 176 . −16.525 −1.061 −0.010 1.00 23.97 . 1 1344 ATOM O O ASN A 176 . −17.395 −1.318 −0.836 1.00 24.00 . 1 1345 ATOM C CB ASN A 176 . −16.172 1.407 0.561 1.00 21.65 . 1 1346 ATOM C CG ASN A 176 . −16.619 2.540 1.504 1.00 19.67 . 1 1347 ATOM O OD1 ASN A 176 . −17.738 2.494 2.076 1.00 21.25 . 1 1348 ATOM N ND2 ASN A 176 . −15.733 3.560 1.685 1.00 21.52 . 1 1349 ATOM N N LEU A 177 . −15.401 −1.768 0.086 1.00 24.48 . 1 1350 ATOM C CA LEU A 177 . −15.160 −2.858 −0.870 1.00 25.58 . 1 1351 ATOM C C LEU A 177 . −16.137 −4.018 −0.590 1.00 24.84 . 1 1352 ATOM O O LEU A 177 . −16.633 −4.690 −1.522 1.00 24.44 . 1 1353 ATOM C CB LEU A 177 . −13.694 −3.352 −0.759 1.00 25.82 . 1 1354 ATOM C CG LEU A 177 . −12.672 −2.452 −1.444 1.00 28.11 . 1 1355 ATOM C CD1 LEU A 177 . −11.249 −2.880 −1.071 1.00 28.82 . 1 1356 ATOM C CD2 LEU A 177 . −12.898 −2.492 −2.900 1.00 28.31 . 1 1357 ATOM N N ALA A 178 . −16.447 −4.271 0.691 1.00 23.91 . 1 1358 ATOM C CA ALA A 178 . −17.411 −5.330 0.996 1.00 23.68 . 1 1359 ATOM C C ALA A 178 . −18.786 −4.975 0.446 1.00 24.05 . 1 1360 ATOM O O ALA A 178 . −19.498 −5.807 −0.096 1.00 22.81 . 1 1361 ATOM C CB ALA A 178 . −17.515 −5.572 2.521 1.00 23.88 . 1 1362 ATOM N N LEU A 179 . −19.150 −3.713 0.612 1.00 22.49 . 1 1363 ATOM C CA LEU A 179 . −20.419 −3.227 0.121 1.00 21.38 . 1 1364 ATOM C C LEU A 179 . −20.499 −3.298 −1.393 1.00 21.79 . 1 1365 ATOM O O LEU A 179 . −21.500 −3.750 −1.926 1.00 22.34 . 1 1366 ATOM C CB LEU A 179 . −20.626 −1.766 0.558 1.00 19.83 . 1 1367 ATOM C CG LEU A 179 . −21.801 −1.099 −0.117 1.00 18.10 . 1 1368 ATOM C CD1 LEU A 179 . −23.080 −1.786 0.403 1.00 19.69 . 1 1369 ATOM C CD2 LEU A 179 . −21.812 0.478 0.174 1.00 20.36 . 1 1370 ATOM N N ARG A 180 . −19.456 −2.896 −2.087 1.00 21.19 . 1 1371 ATOM C CA ARG A 180 . −19.587 −2.879 −3.546 1.00 22.05 . 1 1372 ATOM C C ARG A 180 . −19.661 −4.271 −4.128 1.00 22.26 . 1 1373 ATOM O O ARG A 180 . −20.174 −4.452 −5.260 1.00 23.25 . 1 1374 ATOM C CB ARG A 180 . −18.473 −2.032 −4.178 1.00 21.97 . 1 1375 ATOM C CG ARG A 180 . −17.077 −2.597 −4.049 1.00 24.44 . 1 1376 ATOM C CD ARG A 180 . −16.832 −3.500 −5.288 1.00 25.15 . 1 1377 ATOM N NE ARG A 180 . −15.448 −3.961 −5.338 1.00 24.85 . 1 1378 ATOM C CZ ARG A 180 . −14.443 −3.341 −5.947 1.00 26.97 . 1 1379 ATOM N NH1 ARG A 180 . −14.638 −2.196 −6.616 1.00 25.68 . 1 1380 ATOM N NH2 ARG A 180 . −13.204 −3.856 −5.846 1.00 27.73 . 1 1381 ATOM N N ASP A 181 . −19.102 −5.246 −3.402 1.00 22.34 . 1 1382 ATOM C CA ASP A 181 . −19.165 −6.649 −3.840 1.00 24.55 . 1 1383 ATOM C C ASP A 181 . −20.552 −7.290 −3.616 1.00 25.11 . 1 1384 ATOM O O ASP A 181 . −20.780 −8.480 −3.991 1.00 27.40 . 1 1385 ATOM C CB ASP A 181 . −18.127 −7.496 −3.113 1.00 25.64 . 1 1386 ATOM C CG ASP A 181 . −16.706 −7.267 −3.603 1.00 27.91 . 1 1387 ATOM O OD1 ASP A 181 . −16.500 −6.718 −4.704 1.00 31.93 . 1 1388 ATOM O OD2 ASP A 181 . −15.773 −7.662 −2.868 1.00 31.40 . 1 1389 ATOM N N CYS A 182 . −21.453 −6.559 −2.963 1.00 24.01 . 1 1390 ATOM C CA CYS A 182 . −22.815 −7.048 −2.718 1.00 25.84 . 1 1391 ATOM C C CYS A 182 . −23.735 −6.767 −3.891 1.00 27.53 . 1 1392 ATOM O O CYS A 182 . −24.483 −5.804 −3.892 1.00 24.69 . 1 1393 ATOM C CB CYS A 182 . −23.418 −6.373 −1.509 1.00 27.99 . 1 1394 ATOM S SG CYS A 182 . −22.683 −6.857 0.060 1.00 28.89 . 1 1395 ATOM N N ASP A 183 . −23.719 −7.627 −4.892 1.00 28.46 . 1 1396 ATOM C CA ASP A 183 . −24.587 −7.377 −6.016 1.00 31.48 . 1 1397 ATOM C C ASP A 183 . −26.057 −7.264 −5.687 1.00 31.17 . 1 1398 ATOM O O ASP A 183 . −26.752 −6.495 −6.346 1.00 32.58 . 1 1399 ATOM C CB ASP A 183 . −24.386 −8.440 −7.089 1.00 33.96 . 1 1400 ATOM C CG ASP A 183 . −23.074 −8.280 −7.805 1.00 37.74 . 1 1401 ATOM O OD1 ASP A 183 . −22.819 −7.148 −8.321 1.00 36.86 . 1 1402 ATOM O OD2 ASP A 183 . −22.322 −9.293 −7.844 1.00 38.14 . 1 1403 ATOM N N PHE A 184 . −26.550 −7.988 −4.683 1.00 30.10 . 1 1404 ATOM C CA PHE A 184 . −27.984 −7.910 −4.357 1.00 30.95 . 1 1405 ATOM C C PHE A 184 . −28.402 −6.489 −3.951 1.00 29.79 . 1 1406 ATOM O O PHE A 184 . −29.572 −6.076 −4.093 1.00 30.46 . 1 1407 ATOM C CB PHE A 184 . −28.338 −8.932 −3.261 1.00 30.92 . 1 1408 ATOM C CG PHE A 184 . −27.759 −8.603 −1.907 1.00 31.53 . 1 1409 ATOM C CD1 PHE A 184 . −28.456 −7.789 −1.023 1.00 33.97 . 1 1410 ATOM C CD2 PHE A 184 . −26.501 −9.109 −1.530 1.00 32.62 . 1 1411 ATOM C CE1 PHE A 184 . −27.916 −7.475 0.232 1.00 33.72 . 1 1412 ATOM C CE2 PHE A 184 . −25.949 −8.799 −0.284 1.00 32.55 . 1 1413 ATOM C CZ PHE A 184 . −26.659 −7.980 0.597 1.00 33.21 . 1 1414 ATOM N N VAL A 185 . −27.433 −5.726 −3.441 1.00 28.59 . 1 1415 ATOM C CA VAL A 185 . −27.737 −4.359 −3.090 1.00 25.30 . 1 1416 ATOM C C VAL A 185 . −27.888 −3.465 −4.343 1.00 25.52 . 1 1417 ATOM O O VAL A 185 . −28.828 −2.647 −4.432 1.00 24.74 . 1 1418 ATOM C CB VAL A 185 . −26.612 −3.713 −2.177 1.00 22.73 . 1 1419 ATOM C CG1 VAL A 185 . −26.837 −2.143 −2.091 1.00 22.76 . 1 1420 ATOM C CG2 VAL A 185 . −26.561 −4.381 −0.794 1.00 23.41 . 1 1421 ATOM N N PHE A 186 . −27.021 −3.646 −5.332 1.00 24.63 . 1 1422 ATOM C CA PHE A 186 . −27.024 −2.718 −6.464 1.00 23.83 . 1 1423 ATOM C C PHE A 186 . −27.748 −3.132 −7.728 1.00 25.20 . 1 1424 ATOM O O PHE A 186 . −27.960 −2.324 −8.647 1.00 24.05 . 1 1425 ATOM C CB PHE A 186 . −25.583 −2.357 −6.773 1.00 22.98 . 1 1426 ATOM C CG PHE A 186 . −24.894 −1.664 −5.639 1.00 21.83 . 1 1427 ATOM C CD1 PHE A 186 . −24.183 −2.379 −4.683 1.00 22.14 . 1 1428 ATOM C CD2 PHE A 186 . −25.006 −0.282 −5.508 1.00 24.17 . 1 1429 ATOM C CE1 PHE A 186 . −23.598 −1.695 −3.581 1.00 20.34 . 1 1430 ATOM C CE2 PHE A 186 . −24.430 0.402 −4.423 1.00 23.53 . 1 1431 ATOM C CZ PHE A 186 . −23.746 −0.284 −3.472 1.00 22.36 . 1 1432 ATOM N N ASP A 187 . −28.108 −4.396 −7.778 1.00 26.30 . 1 1433 ATOM C CA ASP A 187 . −28.851 −4.922 −8.913 1.00 29.02 . 1 1434 ATOM C C ASP A 187 . −30.104 −4.106 −9.242 1.00 27.87 . 1 1435 ATOM O O ASP A 187 . −30.925 −3.826 −8.367 1.00 29.57 . 1 1436 ATOM C CB ASP A 187 . −29.321 −6.334 −8.606 1.00 30.63 . 1 1437 ATOM C CG ASP A 187 . −28.256 −7.375 −8.835 1.00 33.25 . 1 1438 ATOM O OD1 ASP A 187 . −27.191 −7.043 −9.424 1.00 35.47 . 1 1439 ATOM O OD2 ASP A 187 . −28.506 −8.544 −8.423 1.00 37.58 . 1 1440 ATOM N N GLY A 188 . −30.225 −3.693 −10.497 1.00 29.07 . 1 1441 ATOM C CA GLY A 188 . −31.402 −2.969 −10.919 1.00 28.39 . 1 1442 ATOM C C GLY A 188 . −31.453 −1.503 −10.569 1.00 28.73 . 1 1443 ATOM O O GLY A 188 . −32.310 −0.786 −11.094 1.00 30.31 . 1 1444 ATOM N N LEU A 189 . −30.544 −1.020 −9.722 1.00 25.99 . 1 1445 ATOM C CA LEU A 189 . −30.593 0.390 −9.367 1.00 24.94 . 1 1446 ATOM C C LEU A 189 . −30.207 1.356 −10.463 1.00 24.70 . 1 1447 ATOM O O LEU A 189 . −29.275 1.113 −11.224 1.00 23.81 . 1 1448 ATOM C CB LEU A 189 . −29.666 0.671 −8.179 1.00 24.21 . 1 1449 ATOM C CG LEU A 189 . −29.995 0.116 −6.792 1.00 24.08 . 1 1450 ATOM C CD1 LEU A 189 . −28.989 0.692 −5.791 1.00 21.45 . 1 1451 ATOM C CD2 LEU A 189 . −31.410 0.508 −6.367 1.00 23.72 . 1 1452 ATOM N N GLU A 190 . −30.919 2.465 −10.544 1.00 25.24 . 1 1453 ATOM C CA GLU A 190 . −30.488 3.479 −11.472 1.00 24.19 . 1 1454 ATOM C C GLU A 190 . −29.909 4.670 −10.701 1.00 22.92 . 1 1455 ATOM O O GLU A 190 . −29.127 5.449 −11.276 1.00 23.06 . 1 1456 ATOM C CB GLU A 190 . −31.627 3.914 −12.367 1.00 27.07 . 1 1457 ATOM C CG GLU A 190 . −32.176 2.751 −13.172 1.00 31.32 . 1 1458 ATOM C CD GLU A 190 . −33.087 3.212 −14.280 1.00 36.71 . 1 1459 ATOM O OE1 GLU A 190 . −33.857 4.156 −14.041 1.00 38.69 . 1 1460 ATOM O OE2 GLU A 190 . −33.042 2.636 −15.394 1.00 38.79 . 1 1461 ATOM N N SER A 191 . −30.227 4.784 −9.408 1.00 21.75 . 1 1462 ATOM C CA SER A 191 . −29.743 5.892 −8.625 1.00 22.92 . 1 1463 ATOM C C SER A 191 . −29.722 5.491 −7.158 1.00 21.94 . 1 1464 ATOM O O SER A 191 . −30.468 4.620 −6.704 1.00 21.24 . 1 1465 ATOM C CB SER A 191 . −30.610 7.148 −8.771 1.00 22.98 . 1 1466 ATOM O OG SER A 191 . −31.974 6.929 −8.398 1.00 24.15 . 1 1467 ATOM N N ILE A 192 . −28.810 6.126 −6.447 1.00 21.51 . 1 1468 ATOM C CA ILE A 192 . −28.700 5.894 −5.007 1.00 20.81 . 1 1469 ATOM C C ILE A 192 . −28.268 7.182 −4.354 1.00 20.62 . 1 1470 ATOM O O ILE A 192 . −27.549 7.984 −4.976 1.00 21.28 . 1 1471 ATOM C CB ILE A 192 . −27.671 4.790 −4.691 1.00 22.11 . 1 1472 ATOM C CG1 ILE A 192 . −27.675 4.480 −3.195 1.00 21.19 . 1 1473 ATOM C CG2 ILE A 192 . −26.256 5.204 −5.206 1.00 23.74 . 1 1474 ATOM C CD1 ILE A 192 . −27.122 3.035 −2.883 1.00 22.84 . 1 1475 ATOM N N VAL A 193 . −28.761 7.443 −3.135 1.00 20.46 . 1 1476 ATOM C CA VAL A 193 . −28.296 8.650 −2.434 1.00 18.90 . 1 1477 ATOM C C VAL A 193 . −27.599 8.125 −1.161 1.00 17.87 . 1 1478 ATOM O O VAL A 193 . −28.183 7.331 −0.413 1.00 18.69 . 1 1479 ATOM C CB VAL A 193 . −29.456 9.692 −2.044 1.00 19.86 . 1 1480 ATOM C CG1 VAL A 193 . −30.609 9.029 −1.248 1.00 20.71 . 1 1481 ATOM C CG2 VAL A 193 . −28.830 10.929 −1.314 1.00 18.89 . 1 1482 ATOM N N ASP A 194 . −26.357 8.547 −0.919 1.00 18.84 . 1 1483 ATOM C CA ASP A 194 . −25.654 8.122 0.313 1.00 18.04 . 1 1484 ATOM C C ASP A 194 . −25.918 9.238 1.337 1.00 17.90 . 1 1485 ATOM O O ASP A 194 . −25.347 10.337 1.240 1.00 19.95 . 1 1486 ATOM C CB ASP A 194 . −24.166 7.951 0.013 1.00 19.12 . 1 1487 ATOM C CG ASP A 194 . −23.411 7.377 1.197 1.00 17.63 . 1 1488 ATOM O OD1 ASP A 194 . −24.120 7.105 2.220 1.00 20.74 . 1 1489 ATOM O OD2 ASP A 194 . −22.132 7.218 1.109 1.00 19.98 . 1 1490 ATOM N N VAL A 195 . −26.857 8.983 2.255 1.00 17.66 . 1 1491 ATOM C CA VAL A 195 . −27.305 9.974 3.254 1.00 18.67 . 1 1492 ATOM C C VAL A 195 . −26.296 9.994 4.400 1.00 19.03 . 1 1493 ATOM O O VAL A 195 . −26.055 8.968 5.054 1.00 19.59 . 1 1494 ATOM C CB VAL A 195 . −28.715 9.601 3.683 1.00 17.97 . 1 1495 ATOM C CG1 VAL A 195 . −29.198 10.492 4.802 1.00 19.57 . 1 1496 ATOM C CG2 VAL A 195 . −29.622 9.725 2.464 1.00 18.87 . 1 1497 ATOM N N GLY A 196 . −25.733 11.174 4.617 1.00 19.64 . 1 1498 ATOM C CA GLY A 196 . −24.647 11.347 5.572 1.00 18.87 . 1 1499 ATOM C C GLY A 196 . −23.421 10.732 4.915 1.00 18.67 . 1 1500 ATOM O O GLY A 196 . −22.582 10.129 5.582 1.00 19.54 . 1 1501 ATOM N N GLY A 197 . −23.292 10.936 3.582 1.00 17.93 . 1 1502 ATOM C CA GLY A 197 . −22.202 10.368 2.803 1.00 17.77 . 1 1503 ATOM C C GLY A 197 . −20.800 10.979 2.906 1.00 17.47 . 1 1504 ATOM O O GLY A 197 . −19.854 10.536 2.196 1.00 20.20 . 1 1505 ATOM N N GLY A 198 . −20.682 11.944 3.789 1.00 18.64 . 1 1506 ATOM C CA GLY A 198 . −19.424 12.628 4.056 1.00 21.17 . 1 1507 ATOM C C GLY A 198 . −18.843 13.353 2.847 1.00 20.80 . 1 1508 ATOM O O GLY A 198 . −19.547 14.117 2.157 1.00 21.83 . 1 1509 ATOM N N THR A 199 . −17.578 13.056 2.565 1.00 22.08 . 1 1510 ATOM C CA THR A 199 . −16.859 13.659 1.452 1.00 23.58 . 1 1511 ATOM C C THR A 199 . −16.957 12.768 0.222 1.00 24.02 . 1 1512 ATOM O O THR A 199 . −16.257 12.951 −0.767 1.00 23.51 . 1 1513 ATOM C CB THR A 199 . −15.346 13.879 1.818 1.00 25.51 . 1 1514 ATOM O OG1 THR A 199 . −14.748 12.635 2.232 1.00 27.01 . 1 1515 ATOM C CG2 THR A 199 . −15.218 14.894 2.947 1.00 28.74 . 1 1516 ATOM N N GLY A 200 . −17.832 11.758 0.305 1.00 24.20 . 1 1517 ATOM C CA GLY A 200 . −17.997 10.882 −0.847 1.00 24.35 . 1 1518 ATOM C C GLY A 200 . −17.096 9.668 −1.002 1.00 23.70 . 1 1519 ATOM O O GLY A 200 . −17.049 9.129 −2.125 1.00 23.45 . 1 1520 ATOM N N THR A 201 . −16.448 9.231 0.082 1.00 23.40 . 1 1521 ATOM C CA THR A 201 . −15.540 8.080 0.050 1.00 24.56 . 1 1522 ATOM C C THR A 201 . −16.201 6.837 −0.472 1.00 24.22 . 1 1523 ATOM O O THR A 201 . −15.671 6.199 −1.426 1.00 23.45 . 1 1524 ATOM C CB THR A 201 . −14.970 7.825 1.413 1.00 26.01 . 1 1525 ATOM O OG1 THR A 201 . −14.439 9.071 1.901 1.00 25.87 . 1 1526 ATOM C CG2 THR A 201 . −13.842 6.783 1.333 1.00 25.93 . 1 1527 ATOM N N THR A 202 . −17.366 6.534 0.126 1.00 21.82 . 1 1528 ATOM C CA THR A 202 . −18.143 5.333 −0.254 1.00 21.15 . 1 1529 ATOM C C THR A 202 . −18.657 5.443 −1.703 1.00 20.95 . 1 1530 ATOM O O THR A 202 . −18.530 4.503 −2.495 1.00 21.71 . 1 1531 ATOM C CB THR A 202 . −19.384 5.138 0.701 1.00 21.31 . 1 1532 ATOM O OG1 THR A 202 . −18.950 4.915 2.064 1.00 20.87 . 1 1533 ATOM C CG2 THR A 202 . −20.171 3.926 0.216 1.00 21.74 . 1 1534 ATOM N N ALA A 203 . −19.255 6.580 −2.026 1.00 21.80 . 1 1535 ATOM C CA ALA A 203 . −19.845 6.851 −3.346 1.00 21.64 . 1 1536 ATOM C C ALA A 203 . −18.843 6.720 −4.445 1.00 21.85 . 1 1537 ATOM O O ALA A 203 . −19.191 6.283 −5.529 1.00 23.72 . 1 1538 ATOM C CB ALA A 203 . −20.436 8.266 −3.352 1.00 22.27 . 1 1539 ATOM N N LYS A 204 . −17.606 7.164 −4.208 1.00 22.97 . 1 1540 ATOM C CA LYS A 204 . −16.579 6.995 −5.232 1.00 23.73 . 1 1541 ATOM C C LYS A 204 . −16.334 5.510 −5.520 1.00 23.28 . 1 1542 ATOM O O LYS A 204 . −16.139 5.145 −6.676 1.00 24.32 . 1 1543 ATOM C CB LYS A 204 . −15.274 7.610 −4.762 1.00 25.89 . 1 1544 ATOM C CG LYS A 204 . −15.337 9.109 −4.760 1.00 29.15 . 1 1545 ATOM C CD LYS A 204 . −14.162 9.698 −3.979 1.00 30.25 . 1 1546 ATOM C CE LYS A 204 . −14.361 11.187 −3.807 1.00 33.67 . 1 1547 ATOM N NZ LYS A 204 . −13.395 11.781 −2.829 1.00 33.96 . 1 1548 ATOM N N ILE A 205 . −16.323 4.671 −4.492 1.00 24.00 . 1 1549 ATOM C CA ILE A 205 . −16.069 3.261 −4.718 1.00 23.77 . 1 1550 ATOM C C ILE A 205 . −17.277 2.678 −5.440 1.00 23.41 . 1 1551 ATOM O O ILE A 205 . −17.141 1.896 −6.374 1.00 23.55 . 1 1552 ATOM C CB ILE A 205 . −15.781 2.541 −3.411 1.00 23.64 . 1 1553 ATOM C CG1 ILE A 205 . −14.367 2.921 −2.952 1.00 26.96 . 1 1554 ATOM C CG2 ILE A 205 . −15.939 1.008 −3.597 1.00 24.40 . 1 1555 ATOM C CD1 ILE A 205 . −14.003 2.381 −1.599 1.00 29.61 . 1 1556 ATOM N N ILE A 206 . −18.462 3.128 −5.055 1.00 21.89 . 1 1557 ATOM C CA ILE A 206 . −19.650 2.643 −5.741 1.00 23.11 . 1 1558 ATOM C C ILE A 206 . −19.599 3.043 −7.219 1.00 23.30 . 1 1559 ATOM O O ILE A 206 . −19.861 2.198 −8.067 1.00 24.23 . 1 1560 ATOM C CB ILE A 206 . −20.957 3.202 −5.124 1.00 21.25 . 1 1561 ATOM C CG1 ILE A 206 . −21.106 2.623 −3.706 1.00 21.21 . 1 1562 ATOM C CG2 ILE A 206 . −22.175 2.858 −6.038 1.00 22.49 . 1 1563 ATOM C CD1 ILE A 206 . −22.293 3.176 −2.935 1.00 24.12 . 1 1564 ATOM N N CYS A 207 . −19.257 4.296 −7.529 1.00 23.63 . 1 1565 ATOM C CA CYS A 207 . −19.254 4.748 −8.920 1.00 24.84 . 1 1566 ATOM C C CYS A 207 . −18.162 4.061 −9.741 1.00 25.87 . 1 1567 ATOM O O CYS A 207 . −18.358 3.829 −10.941 1.00 25.76 . 1 1568 ATOM C CB CYS A 207 . −19.148 6.293 −9.008 1.00 25.36 . 1 1569 ATOM S SG CYS A 207 . −20.595 7.163 −8.422 1.00 30.19 . 1 1570 ATOM N N GLU A 208 . −17.057 3.698 −9.084 1.00 24.68 . 1 1571 ATOM C CA GLU A 208 . −15.942 3.043 −9.755 1.00 24.92 . 1 1572 ATOM C C GLU A 208 . −16.306 1.653 −10.172 1.00 24.00 . 1 1573 ATOM O O GLU A 208 . −15.817 1.173 −11.199 1.00 25.63 . 1 1574 ATOM C CB GLU A 208 . −14.718 3.018 −8.844 1.00 23.89 . 1 1575 ATOM C CG GLU A 208 . −14.001 4.342 −8.918 1.00 28.23 . 1 1576 ATOM C CD GLU A 208 . −13.106 4.602 −7.764 1.00 28.67 . 1 1577 ATOM O OE1 GLU A 208 . −12.807 3.670 −7.003 1.00 29.01 . 1 1578 ATOM O OE2 GLU A 208 . −12.665 5.776 −7.627 1.00 31.89 . 1 1579 ATOM N N THR A 209 . −17.202 1.057 −9.394 1.00 23.88 . 1 1580 ATOM C CA THR A 209 . −17.687 −0.284 −9.586 1.00 23.78 . 1 1581 ATOM C C THR A 209 . −18.862 −0.343 −10.560 1.00 24.67 . 1 1582 ATOM O O THR A 209 . −18.990 −1.321 −11.374 1.00 24.69 . 1 1583 ATOM C CB THR A 209 . −18.128 −0.880 −8.202 1.00 24.81 . 1 1584 ATOM O OG1 THR A 209 . −17.023 −0.811 −7.268 1.00 25.46 . 1 1585 ATOM C CG2 THR A 209 . −18.605 −2.325 −8.355 1.00 25.70 . 1 1586 ATOM N N PHE A 210 . −19.715 0.676 −10.478 1.00 23.56 . 1 1587 ATOM C CA PHE A 210 . −20.942 0.784 −11.277 1.00 25.26 . 1 1588 ATOM C C PHE A 210 . −20.956 2.120 −12.011 1.00 26.64 . 1 1589 ATOM O O PHE A 210 . −21.614 3.097 −11.617 1.00 26.83 . 1 1590 ATOM C CB PHE A 210 . −22.170 0.624 −10.325 1.00 25.67 . 1 1591 ATOM C CG PHE A 210 . −22.140 −0.640 −9.486 1.00 25.08 . 1 1592 ATOM C CD1 PHE A 210 . −21.858 −0.586 −8.112 1.00 24.81 . 1 1593 ATOM C CD2 PHE A 210 . −22.397 −1.901 −10.053 1.00 23.56 . 1 1594 ATOM C CE1 PHE A 210 . −21.836 −1.711 −7.308 1.00 21.95 . 1 1595 ATOM C CE2 PHE A 210 . −22.380 −3.075 −9.250 1.00 26.10 . 1 1596 ATOM C CZ PHE A 210 . −22.101 −2.989 −7.858 1.00 23.44 . 1 1597 ATOM N N PRO A 211 . −20.221 2.186 −13.134 1.00 27.68 . 1 1598 ATOM C CA PRO A 211 . −20.099 3.395 −13.949 1.00 28.40 . 1 1599 ATOM C C PRO A 211 . −21.395 4.037 −14.416 1.00 28.06 . 1 1600 ATOM O O PRO A 211 . −21.414 5.266 −14.623 1.00 30.54 . 1 1601 ATOM C CB PRO A 211 . −19.220 2.935 −15.121 1.00 27.92 . 1 1602 ATOM C CG PRO A 211 . −18.451 1.840 −14.550 1.00 28.20 . 1 1603 ATOM C CD PRO A 211 . −19.507 1.082 −13.774 1.00 29.07 . 1 1604 ATOM N N LYS A 212 . −22.465 3.243 −14.529 1.00 28.42 . 1 1605 ATOM C CA LYS A 212 . −23.745 3.763 −15.025 1.00 28.10 . 1 1606 ATOM C C LYS A 212 . −24.726 4.216 −13.942 1.00 26.85 . 1 1607 ATOM O O LYS A 212 . −25.794 4.767 −14.244 1.00 27.59 . 1 1608 ATOM C CB LYS A 212 . −24.438 2.691 −15.879 1.00 31.43 . 1 1609 ATOM C CG LYS A 212 . −23.555 2.199 −17.053 1.00 32.62 . 1 1610 ATOM C CD LYS A 212 . −24.100 0.931 −17.699 1.00 37.62 . 1 1611 ATOM C CE LYS A 212 . −23.080 0.308 −18.683 1.00 38.96 . 1 1612 ATOM N NZ LYS A 212 . −23.624 −0.922 −19.327 1.00 40.66 . 1 1613 ATOM N N LEU A 213 . −24.369 3.979 −12.683 1.00 24.89 . 1 1614 ATOM C CA LEU A 213 . −25.222 4.340 −11.555 1.00 23.44 . 1 1615 ATOM C C LEU A 213 . −25.114 5.814 −11.131 1.00 24.38 . 1 1616 ATOM O O LEU A 213 . −24.028 6.335 −10.995 1.00 25.29 . 1 1617 ATOM C CB LEU A 213 . −24.858 3.437 −10.388 1.00 23.82 . 1 1618 ATOM C CG LEU A 213 . −25.683 3.514 −9.087 1.00 23.66 . 1 1619 ATOM C CD1 LEU A 213 . −27.135 3.193 −9.347 1.00 22.90 . 1 1620 ATOM C CD2 LEU A 213 . −25.112 2.556 −8.093 1.00 23.73 . 1 1621 ATOM N N LYS A 214 . −26.243 6.471 −10.944 1.00 24.44 . 1 1622 ATOM C CA LYS A 214 . −26.216 7.855 −10.490 1.00 25.02 . 1 1623 ATOM C C LYS A 214 . −26.064 7.790 −8.980 1.00 23.64 . 1 1624 ATOM O O LYS A 214 . −26.830 7.107 −8.303 1.00 23.98 . 1 1625 ATOM C CB LYS A 214 . −27.510 8.593 −10.794 1.00 26.67 . 1 1626 ATOM C CG LYS A 214 . −27.499 9.997 −10.224 1.00 32.78 . 1 1627 ATOM C CD LYS A 214 . −28.799 10.777 −10.353 1.00 35.85 . 1 1628 ATOM C CE LYS A 214 . −28.573 12.187 −9.797 1.00 36.85 . 1 1629 ATOM N NZ LYS A 214 . −29.791 13.036 −10.043 1.00 38.02 . 1 1630 ATOM N N CYS A 215 . −25.085 8.508 −8.453 1.00 23.65 . 1 1631 ATOM C CA CYS A 215 . −24.863 8.519 −7.023 1.00 23.65 . 1 1632 ATOM C C CYS A 215 . −24.879 9.958 −6.524 1.00 22.28 . 1 1633 ATOM O O CYS A 215 . −24.280 10.837 −7.144 1.00 23.29 . 1 1634 ATOM C CB CYS A 215 . −23.511 7.875 −6.727 1.00 24.96 . 1 1635 ATOM S SG CYS A 215 . −23.207 7.598 −5.006 1.00 33.04 . 1 1636 ATOM N N ILE A 216 . −25.614 10.210 −5.447 1.00 20.41 . 1 1637 ATOM C CA ILE A 216 . −25.630 11.566 −4.846 1.00 20.46 . 1 1638 ATOM C C ILE A 216 . −25.038 11.402 −3.431 1.00 20.83 . 1 1639 ATOM O O ILE A 216 . −25.507 10.563 −2.633 1.00 20.91 . 1 1640 ATOM C CB ILE A 216 . −27.064 12.105 −4.683 1.00 21.65 . 1 1641 ATOM C CG1 ILE A 216 . −27.705 12.280 −6.049 1.00 24.77 . 1 1642 ATOM C CG2 ILE A 216 . −27.060 13.415 −3.870 1.00 22.43 . 1 1643 ATOM C CD1 ILE A 216 . −29.238 12.526 −5.954 1.00 26.56 . 1 1644 ATOM N N VAL A 217 . −23.994 12.176 −3.151 1.00 19.13 . 1 1645 ATOM C CA VAL A 217 . −23.383 12.231 −1.814 1.00 18.78 . 1 1646 ATOM C C VAL A 217 . −24.130 13.373 −1.128 1.00 19.47 . 1 1647 ATOM O O VAL A 217 . −24.069 14.515 −1.579 1.00 19.74 . 1 1648 ATOM C CB VAL A 217 . −21.872 12.548 −1.862 1.00 19.68 . 1 1649 ATOM C CG1 VAL A 217 . −21.321 12.665 −0.398 1.00 18.75 . 1 1650 ATOM C CG2 VAL A 217 . −21.154 11.428 −2.627 1.00 19.48 . 1 1651 ATOM N N PHE A 218 . −24.896 13.027 −0.108 1.00 16.97 . 1 1652 ATOM C CA PHE A 218 . −25.721 13.965 0.645 1.00 18.18 . 1 1653 ATOM C C PHE A 218 . −25.212 14.161 2.051 1.00 18.17 . 1 1654 ATOM O O PHE A 218 . −25.135 13.216 2.802 1.00 19.81 . 1 1655 ATOM C CB PHE A 218 . −27.155 13.426 0.671 1.00 18.42 . 1 1656 ATOM C CG PHE A 218 . −28.126 14.330 1.387 1.00 19.48 . 1 1657 ATOM C CD1 PHE A 218 . −28.600 15.476 0.756 1.00 21.39 . 1 1658 ATOM C CD2 PHE A 218 . −28.545 14.025 2.667 1.00 18.95 . 1 1659 ATOM C CE1 PHE A 218 . −29.514 16.301 1.424 1.00 19.67 . 1 1660 ATOM C CE2 PHE A 218 . −29.447 14.815 3.342 1.00 20.45 . 1 1661 ATOM C CZ PHE A 218 . −29.946 15.977 2.724 1.00 20.26 . 1 1662 ATOM N N ASP A 219 . −24.852 15.388 2.425 1.00 18.10 . 1 1663 ATOM C CA ASP A 219 . −24.392 15.599 3.784 1.00 19.70 . 1 1664 ATOM C C ASP A 219 . −24.648 17.082 4.119 1.00 19.39 . 1 1665 ATOM O O ASP A 219 . −25.318 17.769 3.339 1.00 18.10 . 1 1666 ATOM C CB ASP A 219 . −22.908 15.200 3.919 1.00 20.51 . 1 1667 ATOM C CG ASP A 219 . −22.550 14.757 5.335 1.00 20.48 . 1 1668 ATOM O OD1 ASP A 219 . −22.645 15.576 6.292 1.00 21.89 . 1 1669 ATOM O OD2 ASP A 219 . −22.195 13.568 5.545 1.00 19.67 . 1 1670 ATOM N N ARG A 220 . −24.176 17.528 5.279 1.00 19.39 . 1 1671 ATOM C CA ARG A 220 . −24.383 18.936 5.687 1.00 20.97 . 1 1672 ATOM C C ARG A 220 . −23.632 19.851 4.736 1.00 20.98 . 1 1673 ATOM O O ARG A 220 . −22.568 19.512 4.245 1.00 21.01 . 1 1674 ATOM C CB ARG A 220 . −23.952 19.122 7.146 1.00 20.80 . 1 1675 ATOM C CG ARG A 220 . −24.688 18.103 8.027 1.00 21.61 . 1 1676 ATOM C CD ARG A 220 . −24.328 18.197 9.488 1.00 23.54 . 1 1677 ATOM N NE ARG A 220 . −22.908 18.020 9.781 1.00 29.06 . 1 1678 ATOM C CZ ARG A 220 . −22.062 19.034 10.020 1.00 29.81 . 1 1679 ATOM N NH1 ARG A 220 . −22.518 20.284 9.996 1.00 33.47 . 1 1680 ATOM N NH2 ARG A 220 . −20.770 18.801 10.275 1.00 30.40 . 1 1681 ATOM N N PRO A 221 . −24.170 21.072 4.492 1.00 20.82 . 1 1682 ATOM C CA PRO A 221 . −23.553 22.023 3.591 1.00 22.57 . 1 1683 ATOM C C PRO A 221 . −22.058 22.227 3.800 1.00 23.58 . 1 1684 ATOM O O PRO A 221 . −21.289 22.217 2.852 1.00 25.79 . 1 1685 ATOM C CB PRO A 221 . −24.358 23.298 3.836 1.00 23.91 . 1 1686 ATOM C CG PRO A 221 . −25.758 22.763 4.039 1.00 23.46 . 1 1687 ATOM C CD PRO A 221 . −25.455 21.564 4.995 1.00 21.35 . 1 1688 ATOM N N GLN A 222 . −21.656 22.403 5.043 1.00 24.52 . 1 1689 ATOM C CA GLN A 222 . −20.248 22.637 5.299 1.00 25.89 . 1 1690 ATOM C C GLN A 222 . −19.370 21.447 4.954 1.00 26.11 . 1 1691 ATOM O O GLN A 222 . −18.181 21.612 4.669 1.00 27.61 . 1 1692 ATOM C CB GLN A 222 . −20.027 23.055 6.755 1.00 28.52 . 1 1693 ATOM C CG GLN A 222 . −18.578 23.403 6.911 1.00 31.60 . 1 1694 ATOM C CD GLN A 222 . −18.237 24.280 8.087 1.00 33.29 . 1 1695 ATOM O OE1 GLN A 222 . −17.102 24.274 8.509 1.00 36.07 . 1 1696 ATOM N NE2 GLN A 222 . −19.206 25.028 8.624 1.00 34.30 . 1 1697 ATOM N N VAL A 223 . −19.960 20.249 4.947 1.00 23.70 . 1 1698 ATOM C CA VAL A 223 . −19.185 19.066 4.668 1.00 24.46 . 1 1699 ATOM C C VAL A 223 . −18.971 18.900 3.186 1.00 25.11 . 1 1700 ATOM O O VAL A 223 . −17.884 18.539 2.759 1.00 25.99 . 1 1701 ATOM C CB VAL A 223 . −19.878 17.783 5.209 1.00 23.88 . 1 1702 ATOM C CG1 VAL A 223 . −19.148 16.580 4.749 1.00 23.84 . 1 1703 ATOM C CG2 VAL A 223 . −19.968 17.812 6.750 1.00 24.08 . 1 1704 ATOM N N VAL A 224 . −19.978 19.214 2.388 1.00 25.84 . 1 1705 ATOM C CA VAL A 224 . −19.812 19.004 0.947 1.00 27.47 . 1 1706 ATOM C C VAL A 224 . −19.455 20.238 0.141 1.00 29.70 . 1 1707 ATOM O O VAL A 224 . −19.298 20.168 −1.085 1.00 29.16 . 1 1708 ATOM C CB VAL A 224 . −21.077 18.271 0.384 1.00 26.12 . 1 1709 ATOM C CG1 VAL A 224 . −21.285 16.952 1.123 1.00 25.51 . 1 1710 ATOM C CG2 VAL A 224 . −22.304 19.126 0.517 1.00 27.31 . 1 1711 ATOM N N GLU A 225 . −19.294 21.377 0.826 1.00 33.59 . 1 1712 ATOM C CA GLU A 225 . −18.950 22.615 0.133 1.00 36.81 . 1 1713 ATOM C C GLU A 225 . −17.593 22.479 −0.530 1.00 37.55 . 1 1714 ATOM O O GLU A 225 . −16.672 21.874 0.005 1.00 37.45 . 1 1715 ATOM C CB GLU A 225 . −18.967 23.833 1.078 1.00 39.12 . 1 1716 ATOM C CG GLU A 225 . −17.966 23.800 2.237 1.00 41.82 . 1 1717 ATOM C CD GLU A 225 . −17.911 25.142 2.988 1.00 43.01 . 1 1718 ATOM O OE1 GLU A 225 . −18.981 25.700 3.309 1.00 43.70 . 1 1719 ATOM O OE2 GLU A 225 . −16.790 25.638 3.258 1.00 46.07 . 1 1720 ATOM N N ASN A 226 . −17.487 23.029 −1.728 1.00 39.08 . 1 1721 ATOM C CA ASN A 226 . −16.234 22.976 −2.460 1.00 39.38 . 1 1722 ATOM C C ASN A 226 . −15.875 21.621 −3.025 1.00 39.09 . 1 1723 ATOM O O ASN A 226 . −14.816 21.496 −3.647 1.00 38.91 . 1 1724 ATOM C CB ASN A 226 . −15.071 23.459 −1.596 1.00 41.84 . 1 1725 ATOM C CG ASN A 226 . −15.242 24.883 −1.160 1.00 42.73 . 1 1726 ATOM O OD1 ASN A 226 . −15.649 25.722 −1.953 1.00 44.61 . 1 1727 ATOM N ND2 ASN A 226 . −14.926 25.169 0.100 1.00 43.02 . 1 1728 ATOM N N LEU A 227 . −16.690 20.592 −2.779 1.00 36.72 . 1 1729 ATOM C CA LEU A 227 . −16.386 19.314 −3.393 1.00 36.86 . 1 1730 ATOM C C LEU A 227 . −17.011 19.323 −4.779 1.00 37.23 . 1 1731 ATOM O O LEU A 227 . −18.111 19.857 −4.991 1.00 37.71 . 1 1732 ATOM C CB LEU A 227 . −16.930 18.131 −2.565 1.00 34.37 . 1 1733 ATOM C CG LEU A 227 . −16.344 18.015 −1.156 1.00 32.77 . 1 1734 ATOM C CD1 LEU A 227 . −16.870 16.782 −0.473 1.00 33.64 . 1 1735 ATOM C CD2 LEU A 227 . −14.822 17.990 −1.227 1.00 34.05 . 1 1736 ATOM N N SER A 228 . −16.279 18.770 −5.733 1.00 38.85 . 1 1737 ATOM C CA SER A 228 . −16.758 18.681 −7.105 1.00 39.28 . 1 1738 ATOM C C SER A 228 . −16.952 17.218 −7.416 1.00 38.94 . 1 1739 ATOM O O SER A 228 . −16.123 16.368 −7.062 1.00 39.50 . 1 1740 ATOM C CB SER A 228 . −15.744 19.268 −8.098 1.00 40.30 . 1 1741 ATOM O OG SER A 228 . −15.494 20.634 −7.835 1.00 43.33 . 1 1742 ATOM N N GLY A 229 . −18.071 16.926 −8.054 1.00 38.40 . 1 1743 ATOM C CA GLY A 229 . −18.343 15.564 −8.419 1.00 39.54 . 1 1744 ATOM C C GLY A 229 . −17.866 15.408 −9.840 1.00 40.71 . 1 1745 ATOM O O GLY A 229 . −17.102 16.235 −10.372 1.00 41.41 . 1 1746 ATOM N N SER A 230 . −18.320 14.347 −10.476 1.00 41.33 . 1 1747 ATOM C CA SER A 230 . −17.953 14.103 −11.853 1.00 42.15 . 1 1748 ATOM C C SER A 230 . −18.724 12.902 −12.365 1.00 41.51 . 1 1749 ATOM O O SER A 230 . −18.886 11.903 −11.647 1.00 41.00 . 1 1750 ATOM C CB SER A 230 . −16.438 13.880 −11.950 1.00 43.16 . 1 1751 ATOM O OG SER A 230 . −15.994 12.957 −10.959 1.00 45.71 . 1 1752 ATOM N N ASN A 231 . −19.212 13.022 −13.601 1.00 41.61 . 1 1753 ATOM C CA ASN A 231 . −19.982 11.975 −14.272 1.00 40.48 . 1 1754 ATOM C C ASN A 231 . −20.699 11.059 −13.262 1.00 39.05 . 1 1755 ATOM O O ASN A 231 . −20.088 10.297 −12.515 1.00 40.80 . 1 1756 ATOM C CB ASN A 231 . −19.050 11.165 −15.191 1.00 42.93 . 1 1757 ATOM C CG ASN A 231 . −19.784 10.091 −15.987 1.00 43.96 . 1 1758 ATOM O OD1 ASN A 231 . −20.840 10.344 −16.595 1.00 46.47 . 1 1759 ATOM N ND2 ASN A 231 . −19.218 8.879 −15.999 1.00 44.05 . 1 1760 ATOM N N ASN A 232 . −22.011 11.144 −13.264 1.00 36.91 . 1 1761 ATOM C CA ASN A 232 . −22.845 10.377 −12.368 1.00 32.84 . 1 1762 ATOM C C ASN A 232 . −22.686 10.568 −10.876 1.00 31.46 . 1 1763 ATOM O O ASN A 232 . −23.591 10.173 −10.152 1.00 31.53 . 1 1764 ATOM C CB ASN A 232 . −22.797 8.896 −12.690 1.00 32.88 . 1 1765 ATOM C CG ASN A 232 . −23.268 8.618 −14.080 1.00 33.26 . 1 1766 ATOM O OD1 ASN A 232 . −24.050 9.407 −14.657 1.00 33.56 . 1 1767 ATOM N ND2 ASN A 232 . −22.829 7.493 −14.637 1.00 33.88 . 1 1768 ATOM N N LEU A 233 . −21.577 11.144 −10.397 1.00 28.53 . 1 1769 ATOM C CA LEU A 233 . −21.445 11.392 −8.949 1.00 27.58 . 1 1770 ATOM C C LEU A 233 . −21.593 12.906 −8.694 1.00 27.32 . 1 1771 ATOM O O LEU A 233 . −20.855 13.737 −9.244 1.00 28.95 . 1 1772 ATOM C CB LEU A 233 . −20.077 10.901 −8.385 1.00 27.56 . 1 1773 ATOM C CG LEU A 233 . −19.936 10.990 −6.834 1.00 27.15 . 1 1774 ATOM C CD1 LEU A 233 . −18.796 10.051 −6.355 1.00 29.89 . 1 1775 ATOM C CD2 LEU A 233 . −19.642 12.438 −6.385 1.00 29.96 . 1 1776 ATOM N N THR A 234 . −22.537 13.269 −7.860 1.00 25.56 . 1 1777 ATOM C CA THR A 234 . −22.753 14.671 −7.501 1.00 25.62 . 1 1778 ATOM C C THR A 234 . −22.855 14.803 −5.992 1.00 24.73 . 1 1779 ATOM O O THR A 234 . −23.005 13.803 −5.291 1.00 24.73 . 1 1780 ATOM C CB THR A 234 . −24.057 15.238 −8.082 1.00 25.60 . 1 1781 ATOM O OG1 THR A 234 . −25.159 14.387 −7.737 1.00 26.64 . 1 1782 ATOM C CG2 THR A 234 . −23.949 15.371 −9.595 1.00 27.04 . 1 1783 ATOM N N TYR A 235 . −22.697 16.041 −5.507 1.00 22.26 . 1 1784 ATOM C CA TYR A 235 . −22.818 16.352 −4.068 1.00 23.14 . 1 1785 ATOM C C TYR A 235 . −23.990 17.279 −3.849 1.00 22.26 . 1 1786 ATOM O O TYR A 235 . −24.205 18.255 −4.610 1.00 23.85 . 1 1787 ATOM C CB TYR A 235 . −21.556 17.035 −3.509 1.00 22.31 . 1 1788 ATOM C CG TYR A 235 . −20.309 16.160 −3.561 1.00 24.89 . 1 1789 ATOM C CD1 TYR A 235 . −19.560 16.062 −4.719 1.00 24.34 . 1 1790 ATOM C CD2 TYR A 235 . −19.917 15.408 −2.459 1.00 26.40 . 1 1791 ATOM C CE1 TYR A 235 . −18.463 15.258 −4.797 1.00 26.04 . 1 1792 ATOM C CE2 TYR A 235 . −18.819 14.571 −2.522 1.00 25.88 . 1 1793 ATOM C CZ TYR A 235 . −18.092 14.502 −3.700 1.00 28.00 . 1 1794 ATOM O OH TYR A 235 . −16.994 13.622 −3.846 1.00 29.70 . 1 1795 ATOM N N VAL A 236 . −24.769 16.978 −2.810 1.00 21.05 . 1 1796 ATOM C CA VAL A 236 . −25.887 17.804 −2.406 1.00 20.65 . 1 1797 ATOM C C VAL A 236 . −25.801 18.110 −0.935 1.00 20.85 . 1 1798 ATOM O O VAL A 236 . −25.644 17.207 −0.124 1.00 22.46 . 1 1799 ATOM C CB VAL A 236 . −27.236 17.138 −2.704 1.00 19.70 . 1 1800 ATOM C CG1 VAL A 236 . −28.388 17.930 −2.117 1.00 19.75 . 1 1801 ATOM C CG2 VAL A 236 . −27.386 17.058 −4.154 1.00 20.96 . 1 1802 ATOM N N GLY A 237 . −25.817 19.399 −0.608 1.00 19.66 . 1 1803 ATOM C CA GLY A 237 . −25.777 19.824 0.802 1.00 19.78 . 1 1804 ATOM C C GLY A 237 . −27.196 19.956 1.347 1.00 21.28 . 1 1805 ATOM O O GLY A 237 . −28.047 20.513 0.678 1.00 24.81 . 1 1806 ATOM N N GLY A 238 . −27.488 19.415 2.536 1.00 20.14 . 1 1807 ATOM C CA GLY A 238 . −28.826 19.505 3.107 1.00 21.77 . 1 1808 ATOM C C GLY A 238 . −28.890 19.031 4.532 1.00 21.28 . 1 1809 ATOM O O GLY A 238 . −27.860 18.920 5.211 1.00 21.58 . 1 1810 ATOM N N ASP A 239 . −30.106 18.739 4.976 1.00 20.59 . 1 1811 ATOM C CA ASP A 239 . −30.399 18.278 6.318 1.00 20.61 . 1 1812 ATOM C C ASP A 239 . −31.300 17.049 6.177 1.00 20.66 . 1 1813 ATOM O O ASP A 239 . −32.444 17.189 5.751 1.00 19.75 . 1 1814 ATOM C CB ASP A 239 . −31.145 19.388 7.072 1.00 22.89 . 1 1815 ATOM C CG ASP A 239 . −31.465 19.008 8.490 1.00 24.20 . 1 1816 ATOM O OD1 ASP A 239 . −31.236 17.854 8.879 1.00 20.76 . 1 1817 ATOM O OD2 ASP A 239 . −31.998 19.858 9.266 1.00 29.31 . 1 1818 HETA N N MSE A 240 . −30.800 15.867 6.566 1.00 18.85 . 1 1819 HETA C CA MSE A 240 . −31.575 14.643 6.431 1.00 18.69 . 1 1820 HETA C C MSE A 240 . −32.867 14.681 7.262 1.00 19.95 . 1 1821 HETA O O MSE A 240 . −33.787 13.917 7.031 1.00 19.09 . 1 1822 HETA C CB MSE A 240 . −30.696 13.416 6.773 1.00 18.68 . 1 1823 HETA C CG MSE A 240 . −30.291 13.381 8.171 1.00 18.96 . 1 1824 HETA SE SE MSE A 240 . −29.007 11.935 8.437 1.00 11.33 . 1 1825 HETA C CE MSE A 240 . −28.423 12.341 10.377 1.00 20.81 . 1 1826 ATOM N N PHE A 241 . −32.954 15.636 8.184 1.00 20.26 . 1 1827 ATOM C CA PHE A 241 . −34.113 15.724 9.022 1.00 21.94 . 1 1828 ATOM C C PHE A 241 . −35.212 16.543 8.394 1.00 22.14 . 1 1829 ATOM O O PHE A 241 . −36.339 16.564 8.923 1.00 23.25 . 1 1830 ATOM C CB PHE A 241 . −33.743 16.324 10.403 1.00 22.17 . 1 1831 ATOM C CG PHE A 241 . −33.033 15.356 11.301 1.00 21.15 . 1 1832 ATOM C CD1 PHE A 241 . −31.636 15.292 11.307 1.00 21.89 . 1 1833 ATOM C CD2 PHE A 241 . −33.746 14.510 12.159 1.00 21.79 . 1 1834 ATOM C CE1 PHE A 241 . −30.996 14.399 12.163 1.00 21.92 . 1 1835 ATOM C CE2 PHE A 241 . −33.083 13.612 13.022 1.00 23.60 . 1 1836 ATOM C CZ PHE A 241 . −31.719 13.567 13.013 1.00 21.73 . 1 1837 ATOM N N THR A 242 . −34.885 17.183 7.286 1.00 22.38 . 1 1838 ATOM C CA THR A 242 . −35.821 18.029 6.578 1.00 22.62 . 1 1839 ATOM C C THR A 242 . −36.206 17.507 5.174 1.00 21.56 . 1 1840 ATOM O O THR A 242 . −37.377 17.489 4.811 1.00 20.89 . 1 1841 ATOM C CB THR A 242 . −35.217 19.432 6.467 1.00 25.58 . 1 1842 ATOM O OG1 THR A 242 . −35.006 19.953 7.800 1.00 29.05 . 1 1843 ATOM C CG2 THR A 242 . −36.190 20.342 5.706 1.00 26.29 . 1 1844 ATOM N N SER A 243 . −35.216 17.123 4.385 1.00 20.44 . 1 1845 ATOM C CA SER A 243 . −35.506 16.590 3.050 1.00 20.06 . 1 1846 ATOM C C SER A 243 . −34.292 15.890 2.480 1.00 19.87 . 1 1847 ATOM O O SER A 243 . −33.168 16.474 2.479 1.00 20.10 . 1 1848 ATOM C CB SER A 243 . −35.949 17.699 2.068 1.00 22.81 . 1 1849 ATOM O OG SER A 243 . −36.088 17.170 0.743 1.00 24.57 . 1 1850 ATOM N N ILE A 244 . −34.529 14.646 1.997 1.00 19.28 . 1 1851 ATOM C CA ILE A 244 . −33.441 13.841 1.402 1.00 20.00 . 1 1852 ATOM C C ILE A 244 . −33.780 13.705 −0.089 1.00 20.40 . 1 1853 ATOM O O ILE A 244 . −34.924 13.449 −0.457 1.00 21.47 . 1 1854 ATOM C CB ILE A 244 . −33.409 12.451 2.019 1.00 19.82 . 1 1855 ATOM C CG1 ILE A 244 . −32.970 12.571 3.485 1.00 21.37 . 1 1856 ATOM C CG2 ILE A 244 . −32.459 11.522 1.161 1.00 18.94 . 1 1857 ATOM C CD1 ILE A 244 . −33.190 11.338 4.210 1.00 22.00 . 1 1858 ATOM N N PRO A 245 . −32.801 13.898 −0.977 1.00 20.18 . 1 1859 ATOM C CA PRO A 245 . −33.103 13.781 −2.404 1.00 20.30 . 1 1860 ATOM C C PRO A 245 . −33.722 12.455 −2.855 1.00 20.73 . 1 1861 ATOM O O PRO A 245 . −33.383 11.392 −2.328 1.00 21.59 . 1 1862 ATOM C CB PRO A 245 . −31.748 13.981 −3.055 1.00 21.26 . 1 1863 ATOM C CG PRO A 245 . −30.996 14.830 −2.032 1.00 19.79 . 1 1864 ATOM C CD PRO A 245 . −31.402 14.261 −0.732 1.00 21.03 . 1 1865 ATOM N N ASN A 246 . −34.659 12.514 −3.799 1.00 21.57 . 1 1866 ATOM C CA ASN A 246 . −35.257 11.291 −4.377 1.00 21.78 . 1 1867 ATOM C C ASN A 246 . −34.170 10.435 −5.041 1.00 22.44 . 1 1868 ATOM O O ASN A 246 . −33.249 10.944 −5.722 1.00 21.85 . 1 1869 ATOM C CB ASN A 246 . −36.250 11.661 −5.517 1.00 25.64 . 1 1870 ATOM C CG ASN A 246 . −37.526 12.319 −5.041 1.00 26.59 . 1 1871 ATOM O OD1 ASN A 246 . −38.187 13.025 −5.833 1.00 31.13 . 1 1872 ATOM N ND2 ASN A 246 . −37.909 12.100 −3.815 1.00 26.34 . 1 1873 ATOM N N ALA A 247 . −34.311 9.113 −4.862 1.00 20.97 . 1 1874 ATOM C CA ALA A 247 . −33.431 8.115 −5.493 1.00 22.14 . 1 1875 ATOM C C ALA A 247 . −34.107 6.726 −5.416 1.00 21.04 . 1 1876 ATOM O O ALA A 247 . −35.100 6.521 −4.688 1.00 20.57 . 1 1877 ATOM C CB ALA A 247 . −32.054 8.075 −4.812 1.00 22.49 . 1 1878 ATOM N N ASP A 248 . −33.538 5.746 −6.149 1.00 20.42 . 1 1879 ATOM C CA ASP A 248 . −34.043 4.359 −6.119 1.00 21.85 . 1 1880 ATOM C C ASP A 248 . −33.770 3.695 −4.761 1.00 21.20 . 1 1881 ATOM O O ASP A 248 . −34.488 2.768 −4.336 1.00 21.98 . 1 1882 ATOM C CB ASP A 248 . −33.428 3.505 −7.246 1.00 22.91 . 1 1883 ATOM C CG ASP A 248 . −33.936 3.896 −8.633 1.00 25.83 . 1 1884 ATOM O OD1 ASP A 248 . −35.064 4.433 −8.762 1.00 27.79 . 1 1885 ATOM O OD2 ASP A 248 . −33.203 3.652 −9.606 1.00 28.63 . 1 1886 ATOM N N ALA A 249 . −32.709 4.177 −4.092 1.00 20.69 . 1 1887 ATOM C CA ALA A 249 . −32.318 3.661 −2.795 1.00 21.18 . 1 1888 ATOM C C ALA A 249 . −31.531 4.717 −2.002 1.00 19.06 . 1 1889 ATOM O O ALA A 249 . −30.918 5.593 −2.593 1.00 19.33 . 1 1890 ATOM C CB ALA A 249 . −31.410 2.410 −2.992 1.00 22.38 . 1 1891 ATOM N N VAL A 250 . −31.555 4.571 −0.675 1.00 17.27 . 1 1892 ATOM C CA VAL A 250 . −30.807 5.416 0.263 1.00 19.00 . 1 1893 ATOM C C VAL A 250 . −29.820 4.479 0.949 1.00 18.40 . 1 1894 ATOM O O VAL A 250 . −30.176 3.364 1.256 1.00 21.13 . 1 1895 ATOM C CB VAL A 250 . −31.779 5.974 1.321 1.00 18.84 . 1 1896 ATOM C CG1 VAL A 250 . −31.054 6.517 2.561 1.00 20.07 . 1 1897 ATOM C CG2 VAL A 250 . −32.630 7.032 0.658 1.00 21.06 . 1 1898 ATOM N N LEU A 251 . −28.606 4.943 1.194 1.00 17.70 . 1 1899 ATOM C CA LEU A 251 . −27.598 4.190 1.916 1.00 18.35 . 1 1900 ATOM C C LEU A 251 . −27.389 4.960 3.182 1.00 18.26 . 1 1901 ATOM O O LEU A 251 . −27.293 6.211 3.161 1.00 18.58 . 1 1902 ATOM C CB LEU A 251 . −26.267 4.119 1.135 1.00 19.06 . 1 1903 ATOM C CG LEU A 251 . −25.103 3.530 1.977 1.00 17.86 . 1 1904 ATOM C CD1 LEU A 251 . −25.429 2.019 2.220 1.00 21.39 . 1 1905 ATOM C CD2 LEU A 251 . −23.724 3.635 1.277 1.00 19.94 . 1 1906 ATOM N N LEU A 252 . −27.343 4.253 4.304 1.00 18.67 . 1 1907 ATOM C CA LEU A 252 . −27.047 4.919 5.595 1.00 18.78 . 1 1908 ATOM C C LEU A 252 . −25.844 4.167 6.212 1.00 18.66 . 1 1909 ATOM O O LEU A 252 . −26.055 3.144 6.883 1.00 18.52 . 1 1910 ATOM C CB LEU A 252 . −28.230 4.794 6.527 1.00 18.86 . 1 1911 ATOM C CG LEU A 252 . −29.459 5.533 6.026 1.00 17.48 . 1 1912 ATOM C CD1 LEU A 252 . −30.689 5.160 6.827 1.00 16.90 . 1 1913 ATOM C CD2 LEU A 252 . −29.184 7.052 6.184 1.00 19.56 . 1 1914 ATOM N N LYS A 253 . −24.620 4.671 6.007 1.00 18.31 . 1 1915 ATOM C CA LYS A 253 . −23.452 3.962 6.573 1.00 18.45 . 1 1916 ATOM C C LYS A 253 . −22.951 4.670 7.809 1.00 19.05 . 1 1917 ATOM O O LYS A 253 . −22.523 5.818 7.737 1.00 19.71 . 1 1918 ATOM C CB LYS A 253 . −22.350 3.796 5.499 1.00 19.34 . 1 1919 ATOM C CG LYS A 253 . −20.982 3.289 6.027 1.00 20.65 . 1 1920 ATOM C CD LYS A 253 . −20.022 3.106 4.875 1.00 19.70 . 1 1921 ATOM C CE LYS A 253 . −18.587 2.847 5.433 1.00 20.45 . 1 1922 ATOM N NZ LYS A 253 . −17.745 4.122 5.659 1.00 22.95 . 1 1923 ATOM N N TYR A 254 . −22.956 3.952 8.950 1.00 19.59 . 1 1924 ATOM C CA TYR A 254 . −22.523 4.554 10.216 1.00 19.77 . 1 1925 ATOM C C TYR A 254 . −23.344 5.849 10.538 1.00 20.97 . 1 1926 ATOM O O TYR A 254 . −22.817 6.850 11.102 1.00 21.38 . 1 1927 ATOM C CB TYR A 254 . −21.035 4.854 10.064 1.00 20.92 . 1 1928 ATOM C CG TYR A 254 . −20.119 3.714 10.296 1.00 19.78 . 1 1929 ATOM C CD1 TYR A 254 . −18.965 3.621 9.582 1.00 21.74 . 1 1930 ATOM C CD2 TYR A 254 . −20.327 2.847 11.356 1.00 20.55 . 1 1931 ATOM C CE1 TYR A 254 . −17.980 2.695 9.886 1.00 19.20 . 1 1932 ATOM C CE2 TYR A 254 . −19.346 1.904 11.698 1.00 20.95 . 1 1933 ATOM C CZ TYR A 254 . −18.176 1.850 10.955 1.00 20.88 . 1 1934 ATOM O OH TYR A 254 . −17.140 1.020 11.283 1.00 22.46 . 1 1935 ATOM N N ILE A 255 . −24.645 5.826 10.210 1.00 19.08 . 1 1936 ATOM C CA ILE A 255 . −25.511 7.007 10.526 1.00 19.34 . 1 1937 ATOM C C ILE A 255 . −26.430 6.752 11.723 1.00 20.59 . 1 1938 ATOM O O ILE A 255 . −26.409 7.473 12.725 1.00 21.62 . 1 1939 ATOM C CB ILE A 255 . −26.441 7.350 9.327 1.00 19.38 . 1 1940 ATOM C CG1 ILE A 255 . −25.612 7.606 8.080 1.00 18.04 . 1 1941 ATOM C CG2 ILE A 255 . −27.346 8.539 9.659 1.00 18.35 . 1 1942 ATOM C CD1 ILE A 255 . −24.516 8.676 8.243 1.00 18.18 . 1 1943 ATOM N N LEU A 256 . −27.273 5.689 11.631 1.00 19.81 . 1 1944 ATOM C CA LEU A 256 . −28.281 5.463 12.659 1.00 19.38 . 1 1945 ATOM C C LEU A 256 . −27.746 5.186 14.053 1.00 19.37 . 1 1946 ATOM O O LEU A 256 . −28.410 5.497 15.034 1.00 19.95 . 1 1947 ATOM C CB LEU A 256 . −29.265 4.366 12.204 1.00 19.92 . 1 1948 ATOM C CG LEU A 256 . −30.006 4.707 10.880 1.00 21.47 . 1 1949 ATOM C CD1 LEU A 256 . −31.002 3.609 10.559 1.00 21.14 . 1 1950 ATOM C CD2 LEU A 256 . −30.741 5.994 11.035 1.00 21.31 . 1 1951 ATOM N N HIS A 257 . −26.530 4.668 14.153 1.00 20.08 . 1 1952 ATOM C CA HIS A 257 . −26.060 4.351 15.505 1.00 20.91 . 1 1953 ATOM C C HIS A 257 . −25.681 5.633 16.239 1.00 19.79 . 1 1954 ATOM O O HIS A 257 . −25.385 5.598 17.450 1.00 20.88 . 1 1955 ATOM C CB HIS A 257 . −24.862 3.438 15.435 1.00 21.23 . 1 1956 ATOM C CG HIS A 257 . −23.631 4.110 14.949 1.00 21.32 . 1 1957 ATOM N ND1 HIS A 257 . −22.383 3.816 15.469 1.00 21.73 . 1 1958 ATOM C CD2 HIS A 257 . −23.420 5.010 13.951 1.00 21.52 . 1 1959 ATOM C CE1 HIS A 257 . −21.464 4.498 14.811 1.00 20.60 . 1 1960 ATOM N NE2 HIS A 257 . −22.063 5.229 13.884 1.00 21.42 . 1 1961 ATOM N N ASN A 258 . −25.650 6.743 15.509 1.00 19.21 . 1 1962 ATOM C CA ASN A 258 . −25.316 8.041 16.121 1.00 22.11 . 1 1963 ATOM C C ASN A 258 . −26.537 8.764 16.700 1.00 19.36 . 1 1964 ATOM O O ASN A 258 . −26.417 9.939 17.131 1.00 20.61 . 1 1965 ATOM C CB ASN A 258 . −24.710 8.986 15.076 1.00 23.08 . 1 1966 ATOM C CG ASN A 258 . −23.359 8.513 14.525 1.00 25.56 . 1 1967 ATOM O OD1 ASN A 258 . −23.148 8.545 13.331 1.00 31.14 . 1 1968 ATOM N ND2 ASN A 258 . −22.462 8.116 15.381 1.00 25.99 . 1 1969 ATOM N N TRP A 259 . −27.719 8.130 16.729 1.00 20.48 . 1 1970 ATOM C CA TRP A 259 . −28.931 8.801 17.175 1.00 21.54 . 1 1971 ATOM C C TRP A 259 . −29.857 7.989 18.037 1.00 20.68 . 1 1972 ATOM O O TRP A 259 . −29.822 6.741 17.989 1.00 19.34 . 1 1973 ATOM C CB TRP A 259 . −29.783 9.241 15.959 1.00 21.63 . 1 1974 ATOM C CG TRP A 259 . −28.988 10.030 14.993 1.00 21.91 . 1 1975 ATOM C CD1 TRP A 259 . −28.198 9.556 13.956 1.00 21.41 . 1 1976 ATOM C CD2 TRP A 259 . −28.865 11.445 14.971 1.00 21.82 . 1 1977 ATOM N NE1 TRP A 259 . −27.602 10.604 13.299 1.00 22.00 . 1 1978 ATOM C CE2 TRP A 259 . −27.995 11.775 13.899 1.00 22.35 . 1 1979 ATOM C CE3 TRP A 259 . −29.404 12.476 15.756 1.00 22.97 . 1 1980 ATOM C CZ2 TRP A 259 . −27.661 13.097 13.586 1.00 24.31 . 1 1981 ATOM C CZ3 TRP A 259 . −29.079 13.790 15.445 1.00 23.34 . 1 1982 ATOM C CH2 TRP A 259 . −28.211 14.093 14.362 1.00 23.38 . 1 1983 ATOM N N THR A 260 . −30.681 8.682 18.829 1.00 21.50 . 1 1984 ATOM C CA THR A 260 . −31.700 8.019 19.640 1.00 21.02 . 1 1985 ATOM C C THR A 260 . −32.739 7.368 18.741 1.00 21.97 . 1 1986 ATOM O O THR A 260 . −32.782 7.640 17.522 1.00 22.31 . 1 1987 ATOM C CB THR A 260 . −32.456 8.993 20.504 1.00 22.29 . 1 1988 ATOM O OG1 THR A 260 . −32.989 10.047 19.666 1.00 20.69 . 1 1989 ATOM C CG2 THR A 260 . −31.514 9.596 21.543 1.00 21.73 . 1 1990 ATOM N N ASP A 261 . −33.576 6.525 19.342 1.00 22.78 . 1 1991 ATOM C CA ASP A 261 . −34.621 5.847 18.546 1.00 23.74 . 1 1992 ATOM C C ASP A 261 . −35.507 6.973 17.944 1.00 23.87 . 1 1993 ATOM O O ASP A 261 . −35.932 6.924 16.783 1.00 23.38 . 1 1994 ATOM C CB ASP A 261 . −35.508 4.984 19.443 1.00 24.29 . 1 1995 ATOM C CG ASP A 261 . −34.845 3.716 19.937 1.00 25.78 . 1 1996 ATOM O OD1 ASP A 261 . −33.679 3.454 19.581 1.00 23.73 . 1 1997 ATOM O OD2 ASP A 261 . −35.555 2.977 20.719 1.00 31.48 . 1 1998 ATOM N N LYS A 262 . −35.817 7.981 18.741 1.00 23.57 . 1 1999 ATOM C CA LYS A 262 . −36.678 9.075 18.243 1.00 25.22 . 1 2000 ATOM C C LYS A 262 . −36.114 9.775 16.983 1.00 23.73 . 1 2001 ATOM O O LYS A 262 . −36.838 10.019 15.997 1.00 25.36 . 1 2002 ATOM C CB LYS A 262 . −36.915 10.111 19.340 1.00 26.77 . 1 2003 ATOM C CG LYS A 262 . −37.892 11.227 18.926 1.00 30.30 . 1 2004 ATOM C CD LYS A 262 . −38.454 11.953 20.151 1.00 35.91 . 1 2005 ATOM C CE LYS A 262 . −39.394 13.089 19.748 1.00 37.43 . 1 2006 ATOM N NZ LYS A 262 . −40.072 13.704 20.940 1.00 42.28 . 1 2007 ATOM N N ASP A 263 . −34.849 10.156 17.058 1.00 24.02 . 1 2008 ATOM C CA ASP A 263 . −34.213 10.789 15.925 1.00 21.64 . 1 2009 ATOM C C ASP A 263 . −34.099 9.810 14.767 1.00 21.78 . 1 2010 ATOM O O ASP A 263 . −34.244 10.235 13.626 1.00 21.58 . 1 2011 ATOM C CB ASP A 263 . −32.830 11.377 16.324 1.00 22.46 . 1 2012 ATOM C CG ASP A 263 . −32.968 12.707 17.046 1.00 23.85 . 1 2013 ATOM O OD1 ASP A 263 . −34.007 13.357 16.791 1.00 24.24 . 1 2014 ATOM O OD2 ASP A 263 . −32.063 13.122 17.827 1.00 21.57 . 1 2015 ATOM N N CYS A 264 . −33.847 8.526 15.028 1.00 20.44 . 1 2016 ATOM C CA CYS A 264 . −33.758 7.545 13.950 1.00 20.46 . 1 2017 ATOM C C CYS A 264 . −35.094 7.450 13.215 1.00 19.05 . 1 2018 ATOM O O CYS A 264 . −35.120 7.330 11.989 1.00 19.20 . 1 2019 ATOM C CB CYS A 264 . −33.384 6.153 14.483 1.00 19.50 . 1 2020 ATOM S SG CYS A 264 . −31.621 5.932 14.826 1.00 22.71 . 1 2021 ATOM N N LEU A 265 . −36.198 7.516 13.952 1.00 19.90 . 1 2022 ATOM C CA LEU A 265 . −37.519 7.468 13.319 1.00 20.72 . 1 2023 ATOM C C LEU A 265 . −37.671 8.677 12.403 1.00 21.24 . 1 2024 ATOM O O LEU A 265 . −38.167 8.559 11.263 1.00 21.62 . 1 2025 ATOM C CB LEU A 265 . −38.662 7.425 14.341 1.00 22.17 . 1 2026 ATOM C CG LEU A 265 . −38.754 6.153 15.203 1.00 23.38 . 1 2027 ATOM C CD1 LEU A 265 . −39.889 6.315 16.206 1.00 26.14 . 1 2028 ATOM C CD2 LEU A 265 . −38.951 4.886 14.321 1.00 24.94 . 1 2029 ATOM N N ARG A 266 . −37.226 9.832 12.872 1.00 21.79 . 1 2030 ATOM C CA ARG A 266 . −37.297 11.008 12.016 1.00 21.48 . 1 2031 ATOM C C ARG A 266 . −36.478 10.810 10.731 1.00 20.27 . 1 2032 ATOM O O ARG A 266 . −36.920 11.168 9.638 1.00 20.52 . 1 2033 ATOM C CB ARG A 266 . −36.804 12.239 12.777 1.00 21.47 . 1 2034 ATOM C CG ARG A 266 . −37.666 12.538 13.965 1.00 23.57 . 1 2035 ATOM C CD ARG A 266 . −37.168 13.779 14.698 1.00 32.39 . 1 2036 ATOM N NE ARG A 266 . −38.034 14.066 15.842 1.00 36.68 . 1 2037 ATOM C CZ ARG A 266 . −37.594 14.685 16.930 1.00 38.68 . 1 2038 ATOM N NH1 ARG A 266 . −36.322 15.058 16.980 1.00 41.23 . 1 2039 ATOM N NH2 ARG A 266 . −38.408 14.947 17.946 1.00 39.28 . 1 2040 ATOM N N ILE A 267 . −35.257 10.322 10.867 1.00 20.00 . 1 2041 ATOM C CA ILE A 267 . −34.419 10.083 9.691 1.00 20.12 . 1 2042 ATOM C C ILE A 267 . −35.081 9.033 8.758 1.00 20.20 . 1 2043 ATOM O O ILE A 267 . −35.173 9.229 7.539 1.00 20.97 . 1 2044 ATOM C CB ILE A 267 . −33.038 9.546 10.084 1.00 18.00 . 1 2045 ATOM C CG1 ILE A 267 . −32.212 10.638 10.750 1.00 18.60 . 1 2046 ATOM C CG2 ILE A 267 . −32.304 9.031 8.849 1.00 18.20 . 1 2047 ATOM C CD1 ILE A 267 . −31.031 10.077 11.608 1.00 17.43 . 1 2048 ATOM N N LEU A 268 . −35.496 7.932 9.345 1.00 20.70 . 1 2049 ATOM C CA LEU A 268 . −36.099 6.867 8.561 1.00 20.95 . 1 2050 ATOM C C LEU A 268 . −37.349 7.338 7.825 1.00 22.08 . 1 2051 ATOM O O LEU A 268 . −37.588 6.899 6.651 1.00 20.68 . 1 2052 ATOM C CB LEU A 268 . −36.359 5.645 9.443 1.00 22.24 . 1 2053 ATOM C CG LEU A 268 . −35.140 4.806 9.787 1.00 22.30 . 1 2054 ATOM C CD1 LEU A 268 . −35.592 3.758 10.853 1.00 24.39 . 1 2055 ATOM C CD2 LEU A 268 . −34.568 4.156 8.533 1.00 23.47 . 1 2056 ATOM N N LYS A 269 . −38.137 8.247 8.434 1.00 21.36 . 1 2057 ATOM C CA LYS A 269 . −39.319 8.781 7.749 1.00 22.49 . 1 2058 ATOM C C LYS A 269 . −38.901 9.556 6.471 1.00 22.63 . 1 2059 ATOM O O LYS A 269 . −39.542 9.435 5.431 1.00 22.57 . 1 2060 ATOM C CB LYS A 269 . −40.127 9.698 8.674 1.00 23.50 . 1 2061 ATOM C CG LYS A 269 . −41.394 10.303 7.970 1.00 29.63 . 1 2062 ATOM C CD LYS A 269 . −42.137 11.322 8.838 1.00 32.83 . 1 2063 ATOM C CE LYS A 269 . −43.627 11.340 8.459 1.00 35.82 . 1 2064 ATOM N NZ LYS A 269 . −44.429 12.530 8.999 1.00 37.93 . 1 2065 ATOM N N LYS A 270 . −37.834 10.368 6.547 1.00 21.60 . 1 2066 ATOM C CA LYS A 270 . −37.380 11.105 5.389 1.00 22.24 . 1 2067 ATOM C C LYS A 270 . −36.785 10.181 4.361 1.00 21.64 . 1 2068 ATOM O O LYS A 270 . −36.844 10.474 3.130 1.00 21.66 . 1 2069 ATOM C CB LYS A 270 . −36.385 12.190 5.814 1.00 22.94 . 1 2070 ATOM C CG LYS A 270 . −37.050 13.275 6.702 1.00 23.82 . 1 2071 ATOM C CD LYS A 270 . −38.078 14.084 5.940 1.00 25.76 . 1 2072 ATOM C CE LYS A 270 . −38.589 15.254 6.771 1.00 27.58 . 1 2073 ATOM N NZ LYS A 270 . −39.554 16.067 5.974 1.00 29.04 . 1 2074 ATOM N N CYS A 271 . −36.183 9.085 4.832 1.00 20.60 . 1 2075 ATOM C CA CYS A 271 . −35.627 8.145 3.887 1.00 20.87 . 1 2076 ATOM C C CYS A 271 . −36.746 7.438 3.103 1.00 20.32 . 1 2077 ATOM O O CYS A 271 . −36.640 7.235 1.846 1.00 19.78 . 1 2078 ATOM C CB CYS A 271 . −34.747 7.101 4.615 1.00 20.39 . 1 2079 ATOM S SG CYS A 271 . −33.242 7.710 5.244 1.00 19.96 . 1 2080 ATOM N N LYS A 272 . −37.803 7.050 3.834 1.00 21.28 . 1 2081 ATOM C CA LYS A 272 . −38.916 6.378 3.201 1.00 23.10 . 1 2082 ATOM C C LYS A 272 . −39.523 7.284 2.135 1.00 22.83 . 1 2083 ATOM O O LYS A 272 . −39.831 6.832 1.004 1.00 23.33 . 1 2084 ATOM C CB LYS A 272 . −39.958 5.953 4.248 1.00 22.71 . 1 2085 ATOM C CG LYS A 272 . −41.106 5.213 3.586 1.00 22.99 . 1 2086 ATOM C CD LYS A 272 . −41.978 4.475 4.548 1.00 27.05 . 1 2087 ATOM C CE LYS A 272 . −42.507 5.363 5.610 1.00 30.73 . 1 2088 ATOM N NZ LYS A 272 . −43.424 4.504 6.406 1.00 34.02 . 1 2089 ATOM N N GLU A 273 . −39.658 8.566 2.470 1.00 23.16 . 1 2090 ATOM C CA GLU A 273 . −40.215 9.549 1.550 1.00 24.18 . 1 2091 ATOM C C GLU A 273 . −39.370 9.563 0.270 1.00 23.53 . 1 2092 ATOM O O GLU A 273 . −39.897 9.509 −0.854 1.00 23.83 . 1 2093 ATOM C CB GLU A 273 . −40.092 10.898 2.192 1.00 26.36 . 1 2094 ATOM C CG GLU A 273 . −41.292 11.506 2.839 1.00 34.38 . 1 2095 ATOM C CD GLU A 273 . −40.902 12.860 3.450 1.00 36.72 . 1 2096 ATOM O OE1 GLU A 273 . −40.239 13.673 2.716 1.00 38.05 . 1 2097 ATOM O OE2 GLU A 273 . −41.232 13.087 4.650 1.00 38.71 . 1 2098 ATOM N N ALA A 274 . −38.045 9.647 0.449 1.00 21.03 . 1 2099 ATOM C CA ALA A 274 . −37.100 9.733 −0.661 1.00 20.44 . 1 2100 ATOM C C ALA A 274 . −37.156 8.586 −1.651 1.00 21.56 . 1 2101 ATOM O O ALA A 274 . −36.873 8.777 −2.849 1.00 22.83 . 1 2102 ATOM C CB ALA A 274 . −35.648 9.916 −0.103 1.00 20.35 . 1 2103 ATOM N N VAL A 275 . −37.527 7.404 −1.157 1.00 21.34 . 1 2104 ATOM C CA VAL A 275 . −37.575 6.231 −2.021 1.00 22.75 . 1 2105 ATOM C C VAL A 275 . −39.006 5.846 −2.396 1.00 23.08 . 1 2106 ATOM O O VAL A 275 . −39.236 4.796 −2.967 1.00 23.84 . 1 2107 ATOM C CB VAL A 275 . −36.770 5.024 −1.395 1.00 21.96 . 1 2108 ATOM C CG1 VAL A 275 . −35.295 5.461 −1.060 1.00 21.09 . 1 2109 ATOM C CG2 VAL A 275 . −37.422 4.520 −0.109 1.00 21.77 . 1 2110 ATOM N N THR A 276 . −39.964 6.707 −2.107 1.00 23.21 . 1 2111 ATOM C CA THR A 276 . −41.350 6.405 −2.479 1.00 25.04 . 1 2112 ATOM C C THR A 276 . −42.045 7.521 −3.234 1.00 27.40 . 1 2113 ATOM O O THR A 276 . −43.278 7.548 −3.302 1.00 28.48 . 1 2114 ATOM C CB THR A 276 . −42.226 6.027 −1.293 1.00 23.90 . 1 2115 ATOM O OG1 THR A 276 . −42.223 7.088 −0.333 1.00 24.75 . 1 2116 ATOM C CG2 THR A 276 . −41.773 4.741 −0.698 1.00 23.70 . 1 2117 ATOM N N ASN A 277 . −41.271 8.422 −3.820 1.00 29.59 . 1 2118 ATOM C CA ASN A 277 . −41.847 9.528 −4.597 1.00 34.28 . 1 2119 ATOM C C ASN A 277 . −42.273 9.050 −6.025 1.00 36.67 . 1 2120 ATOM O O ASN A 277 . −41.644 8.147 −6.615 1.00 37.85 . 1 2121 ATOM C CB ASN A 277 . −40.788 10.642 −4.690 1.00 35.92 . 1 2122 ATOM C CG ASN A 277 . −41.113 11.727 −5.733 1.00 38.83 . 1 2123 ATOM O OD1 ASN A 277 . −41.492 12.864 −5.379 1.00 40.81 . 1 2124 ATOM N ND2 ASN A 277 . −40.928 11.401 −7.018 1.00 40.00 . 1 2125 ATOM N N ASP A 278 . −43.342 9.628 −6.568 1.00 39.47 . 1 2126 ATOM C CA ASP A 278 . −43.755 9.300 −7.945 1.00 41.57 . 1 2127 ATOM C C ASP A 278 . −44.347 7.892 −8.085 1.00 40.95 . 1 2128 ATOM O O ASP A 278 . −44.397 7.324 −9.183 1.00 43.62 . 1 2129 ATOM C CB ASP A 278 . −42.522 9.457 −8.870 1.00 43.76 . 1 2130 ATOM C CG ASP A 278 . −42.846 9.237 −10.359 1.00 46.27 . 1 2131 ATOM O OD1 ASP A 278 . −43.961 9.614 −10.825 1.00 47.11 . 1 2132 ATOM O OD2 ASP A 278 . −41.956 8.705 −11.069 1.00 47.04 . 1 2133 ATOM N N GLY A 279 . −44.813 7.333 −6.979 1.00 39.93 . 1 2134 ATOM C CA GLY A 279 . −45.347 5.987 −7.042 1.00 37.52 . 1 2135 ATOM C C GLY A 279 . −44.231 4.931 −7.040 1.00 36.62 . 1 2136 ATOM O O GLY A 279 . −44.510 3.737 −7.180 1.00 35.45 . 1 2137 ATOM N N LYS A 280 . −42.967 5.352 −6.920 1.00 33.94 . 1 2138 ATOM C CA LYS A 280 . −41.870 4.378 −6.899 1.00 32.65 . 1 2139 ATOM C C LYS A 280 . −41.827 3.648 −5.557 1.00 29.75 . 1 2140 ATOM O O LYS A 280 . −42.343 4.145 −4.550 1.00 29.59 . 1 2141 ATOM C CB LYS A 280 . −40.524 5.067 −7.143 1.00 34.08 . 1 2142 ATOM C CG LYS A 280 . −40.220 5.349 −8.633 1.00 35.21 . 1 2143 ATOM C CD LYS A 280 . −38.915 6.141 −8.748 1.00 38.06 . 1 2144 ATOM C CE LYS A 280 . −38.685 6.759 −10.158 1.00 39.31 . 1 2145 ATOM N NZ LYS A 280 . −38.291 5.781 −11.219 1.00 40.44 . 1 2146 ATOM N N ARG A 281 . −41.243 2.448 −5.542 1.00 27.30 . 1 2147 ATOM C CA ARG A 281 . −41.126 1.711 −4.284 1.00 25.64 . 1 2148 ATOM C C ARG A 281 . −39.688 1.215 −4.164 1.00 24.87 . 1 2149 ATOM O O ARG A 281 . −39.385 0.060 −4.505 1.00 25.85 . 1 2150 ATOM C CB ARG A 281 . −42.083 0.524 −4.250 1.00 27.67 . 1 2151 ATOM C CG ARG A 281 . −43.499 0.864 −4.629 1.00 29.76 . 1 2152 ATOM C CD ARG A 281 . −44.075 1.785 −3.631 1.00 30.34 . 1 2153 ATOM N NE ARG A 281 . −43.935 1.238 −2.289 1.00 30.13 . 1 2154 ATOM C CZ ARG A 281 . −44.350 1.872 −1.199 1.00 32.25 . 1 2155 ATOM N NH1 ARG A 281 . −44.931 3.070 −1.302 1.00 33.70 . 1 2156 ATOM N NH2 ARG A 281 . −44.193 1.311 −0.002 1.00 33.33 . 1 2157 ATOM N N GLY A 282 . −38.808 2.089 −3.642 1.00 21.57 . 1 2158 ATOM C CA GLY A 282 . −37.410 1.712 −3.504 1.00 22.44 . 1 2159 ATOM C C GLY A 282 . −37.083 1.027 −2.176 1.00 21.37 . 1 2160 ATOM O O GLY A 282 . −37.939 0.337 −1.575 1.00 22.01 . 1 2161 ATOM N N LYS A 283 . −35.849 1.216 −1.702 1.00 21.39 . 1 2162 ATOM C CA LYS A 283 . −35.420 0.604 −0.438 1.00 20.69 . 1 2163 ATOM C C LYS A 283 . −34.345 1.460 0.254 1.00 21.17 . 1 2164 ATOM O O LYS A 283 . −33.760 2.349 −0.324 1.00 19.78 . 1 2165 ATOM C CB LYS A 283 . −34.794 −0.803 −0.647 1.00 20.96 . 1 2166 ATOM C CG LYS A 283 . −33.512 −0.789 −1.548 1.00 22.56 . 1 2167 ATOM C CD LYS A 283 . −32.773 −2.125 −1.705 1.00 27.41 . 1 2168 ATOM C CE LYS A 283 . −31.577 −1.959 −2.683 1.00 26.83 . 1 2169 ATOM N NZ LYS A 283 . −30.930 −3.255 −2.981 1.00 30.57 . 1 2170 ATOM N N VAL A 284 . −34.100 1.120 1.507 1.00 20.49 . 1 2171 ATOM C CA VAL A 284 . −33.060 1.813 2.275 1.00 18.93 . 1 2172 ATOM C C VAL A 284 . −32.078 0.710 2.734 1.00 19.08 . 1 2173 ATOM O O VAL A 284 . −32.502 −0.357 3.215 1.00 21.18 . 1 2174 ATOM C CB VAL A 284 . −33.708 2.526 3.473 1.00 18.27 . 1 2175 ATOM C CG1 VAL A 284 . −32.631 3.323 4.294 1.00 19.73 . 1 2176 ATOM C CG2 VAL A 284 . −34.821 3.494 2.921 1.00 17.51 . 1 2177 ATOM N N THR A 285 . −30.795 0.962 2.511 1.00 18.26 . 1 2178 ATOM C CA THR A 285 . −29.681 0.036 2.880 1.00 19.59 . 1 2179 ATOM C C THR A 285 . −28.910 0.681 4.041 1.00 20.07 . 1 2180 ATOM O O THR A 285 . −28.550 1.859 3.970 1.00 20.48 . 1 2181 ATOM C CB THR A 285 . −28.784 −0.161 1.671 1.00 21.78 . 1 2182 ATOM O OG1 THR A 285 . −29.587 −0.706 0.602 1.00 22.69 . 1 2183 ATOM C CG2 THR A 285 . −27.716 −1.172 2.001 1.00 21.12 . 1 2184 ATOM N N ILE A 286 . −28.718 −0.070 5.122 1.00 19.56 . 1 2185 ATOM C CA ILE A 286 . −28.064 0.435 6.358 1.00 19.58 . 1 2186 ATOM C C ILE A 286 . −26.827 −0.386 6.624 1.00 20.18 . 1 2187 ATOM O O ILE A 286 . −26.851 −1.599 6.464 1.00 19.80 . 1 2188 ATOM C CB ILE A 286 . −29.056 0.241 7.568 1.00 18.78 . 1 2189 ATOM C CG1 ILE A 286 . −30.281 1.159 7.372 1.00 18.21 . 1 2190 ATOM C CG2 ILE A 286 . −28.367 0.463 8.919 1.00 18.94 . 1 2191 ATOM C CD1 ILE A 286 . −31.463 0.768 8.209 1.00 20.78 . 1 2192 ATOM N N ILE A 287 . −25.737 0.276 7.002 1.00 19.36 . 1 2193 ATOM C CA ILE A 287 . −24.525 −0.424 7.415 1.00 20.61 . 1 2194 ATOM C C ILE A 287 . −24.244 0.083 8.843 1.00 22.23 . 1 2195 ATOM O O ILE A 287 . −23.974 1.295 9.083 1.00 21.69 . 1 2196 ATOM C CB ILE A 287 . −23.313 −0.122 6.499 1.00 21.18 . 1 2197 ATOM C CG1 ILE A 287 . −23.504 −0.736 5.123 1.00 20.14 . 1 2198 ATOM C CG2 ILE A 287 . −22.007 −0.734 7.103 1.00 21.34 . 1 2199 ATOM C CD1 ILE A 287 . −22.493 −0.207 4.145 1.00 22.68 . 1 2200 ATOM N N ASP A 288 . −24.352 −0.857 9.796 1.00 22.17 . 1 2201 ATOM C CA ASP A 288 . −24.107 −0.577 11.237 1.00 21.94 . 1 2202 ATOM C C ASP A 288 . −24.005 −1.911 11.962 1.00 21.03 . 1 2203 ATOM O O ASP A 288 . −24.230 −2.980 11.336 1.00 21.86 . 1 2204 ATOM C CB ASP A 288 . −25.234 0.283 11.837 1.00 21.53 . 1 2205 ATOM C CG ASP A 288 . −24.836 1.769 12.036 1.00 21.00 . 1 2206 ATOM O OD1 ASP A 288 . −23.623 2.061 12.289 1.00 21.11 . 1 2207 ATOM O OD2 ASP A 288 . −25.771 2.630 11.909 1.00 20.81 . 1 2208 HETA N N MSE A 289 . −23.620 −1.882 13.232 1.00 20.22 . 1 2209 HETA C CA MSE A 289 . −23.562 −3.149 13.959 1.00 22.16 . 1 2210 HETA C C MSE A 289 . −24.961 −3.691 14.278 1.00 21.51 . 1 2211 HETA O O MSE A 289 . −25.937 −2.939 14.486 1.00 21.60 . 1 2212 HETA C CB MSE A 289 . −22.805 −2.984 15.297 1.00 18.00 . 1 2213 HETA C CG MSE A 289 . −21.407 −2.612 15.111 1.00 20.30 . 1 2214 HETA SE SE MSE A 289 . −20.714 −2.260 16.906 1.00 14.00 . 1 2215 HETA C CE MSE A 289 . −18.813 −2.311 16.613 1.00 27.60 . 1 2216 ATOM N N VAL A 290 . −25.024 −5.025 14.381 1.00 23.81 . 1 2217 ATOM C CA VAL A 290 . −26.251 −5.717 14.838 1.00 23.25 . 1 2218 ATOM C C VAL A 290 . −25.768 −6.623 15.990 1.00 24.84 . 1 2219 ATOM O O VAL A 290 . −25.048 −7.609 15.749 1.00 24.92 . 1 2220 ATOM C CB VAL A 290 . −26.890 −6.674 13.801 1.00 23.57 . 1 2221 ATOM C CG1 VAL A 290 . −28.097 −7.355 14.427 1.00 25.00 . 1 2222 ATOM C CG2 VAL A 290 . −27.341 −5.922 12.583 1.00 24.02 . 1 2223 ATOM N N ILE A 291 . −26.129 −6.284 17.221 1.00 23.34 . 1 2224 ATOM C CA ILE A 291 . −25.766 −7.110 18.346 1.00 25.69 . 1 2225 ATOM C C ILE A 291 . −26.594 −8.402 18.277 1.00 26.03 . 1 2226 ATOM O O ILE A 291 . −27.784 −8.347 17.972 1.00 26.03 . 1 2227 ATOM C CB ILE A 291 . −26.049 −6.385 19.667 1.00 25.72 . 1 2228 ATOM C CG1 ILE A 291 . −24.989 −5.278 19.827 1.00 24.94 . 1 2229 ATOM C CG2 ILE A 291 . −26.051 −7.402 20.828 1.00 28.62 . 1 2230 ATOM C CD1 ILE A 291 . −25.136 −4.407 21.086 1.00 24.98 . 1 2231 ATOM N N ASP A 292 . −25.956 −9.540 18.564 1.00 28.41 . 1 2232 ATOM C CA ASP A 292 . −26.634 −10.831 18.539 1.00 31.47 . 1 2233 ATOM C C ASP A 292 . −25.960 −11.736 19.584 1.00 31.99 . 1 2234 ATOM O O ASP A 292 . −25.057 −12.482 19.252 1.00 30.75 . 1 2235 ATOM C CB ASP A 292 . −26.482 −11.475 17.151 1.00 33.46 . 1 2236 ATOM C CG ASP A 292 . −27.453 −12.632 16.934 1.00 35.64 . 1 2237 ATOM O OD1 ASP A 292 . −27.900 −13.230 17.935 1.00 34.89 . 1 2238 ATOM O OD2 ASP A 292 . −27.757 −12.944 15.756 1.00 37.63 . 1 2239 ATOM N N LYS A 293 . −26.388 −11.637 20.841 1.00 33.55 . 1 2240 ATOM C CA LYS A 293 . −25.786 −12.429 21.916 1.00 35.26 . 1 2241 ATOM C C LYS A 293 . −25.793 −13.935 21.681 1.00 36.84 . 1 2242 ATOM O O LYS A 293 . −24.846 −14.641 22.054 1.00 37.41 . 1 2243 ATOM C CB LYS A 293 . −26.462 −12.101 23.247 1.00 35.27 . 1 2244 ATOM C CG LYS A 293 . −26.271 −10.624 23.659 1.00 35.74 . 1 2245 ATOM C CD LYS A 293 . −26.842 −10.388 25.029 1.00 36.86 . 1 2246 ATOM C CE LYS A 293 . −26.790 −8.932 25.448 1.00 37.37 . 1 2247 ATOM N NZ LYS A 293 . −27.600 −8.782 26.719 1.00 38.82 . 1 2248 ATOM N N LYS A 294 . −26.834 −14.458 21.064 1.00 37.62 . 1 2249 ATOM C CA LYS A 294 . −26.797 −15.900 20.859 1.00 39.26 . 1 2250 ATOM C C LYS A 294 . −25.946 −16.390 19.681 1.00 39.70 . 1 2251 ATOM O O LYS A 294 . −25.396 −17.490 19.723 1.00 40.44 . 1 2252 ATOM C CB LYS A 294 . −28.213 −16.466 20.761 1.00 41.74 . 1 2253 ATOM C CG LYS A 294 . −29.244 −15.511 20.264 1.00 44.57 . 1 2254 ATOM C CD LYS A 294 . −30.475 −15.638 21.147 1.00 46.23 . 1 2255 ATOM C CE LYS A 294 . −31.574 −14.653 20.735 1.00 47.14 . 1 2256 ATOM N NZ LYS A 294 . −32.786 −14.836 21.604 1.00 47.93 . 1 2257 ATOM N N LYS A 295 . −25.790 −15.581 18.645 1.00 39.58 . 1 2258 ATOM C CA LYS A 295 . −25.029 −16.034 17.488 1.00 39.62 . 1 2259 ATOM C C LYS A 295 . −23.580 −15.596 17.426 1.00 39.22 . 1 2260 ATOM O O LYS A 295 . −22.734 −16.318 16.889 1.00 38.04 . 1 2261 ATOM C CB LYS A 295 . −25.718 −15.596 16.191 1.00 41.62 . 1 2262 ATOM C CG LYS A 295 . −27.213 −15.814 16.176 1.00 43.11 . 1 2263 ATOM C CD LYS A 295 . −27.603 −17.257 16.345 1.00 46.00 . 1 2264 ATOM C CE LYS A 295 . −29.099 −17.351 16.644 1.00 46.57 . 1 2265 ATOM N NZ LYS A 295 . −29.590 −18.767 16.714 1.00 48.69 . 1 2266 ATOM N N ASP A 296 . −23.288 −14.408 17.939 1.00 36.37 . 1 2267 ATOM C CA ASP A 296 . −21.920 −13.923 17.893 1.00 36.59 . 1 2268 ATOM C C ASP A 296 . −20.994 −14.600 18.893 1.00 36.07 . 1 2269 ATOM O O ASP A 296 . −21.425 −15.074 19.955 1.00 34.20 . 1 2270 ATOM C CB ASP A 296 . −21.867 −12.412 18.172 1.00 35.46 . 1 2271 ATOM C CG ASP A 296 . −22.320 −11.572 16.998 1.00 37.53 . 1 2272 ATOM O OD1 ASP A 296 . −22.595 −12.131 15.908 1.00 35.84 . 1 2273 ATOM O OD2 ASP A 296 . −22.383 −10.334 17.186 1.00 34.10 . 1 2274 ATOM N N GLU A 297 . −19.716 −14.605 18.535 1.00 36.52 . 1 2275 ATOM C CA GLU A 297 . −18.652 −15.134 19.371 1.00 37.71 . 1 2276 ATOM C C GLU A 297 . −18.707 −14.187 20.572 1.00 37.57 . 1 2277 ATOM O O GLU A 297 . −18.895 −12.992 20.382 1.00 36.09 . 1 2278 ATOM C CB GLU A 297 . −17.315 −14.950 18.648 1.00 39.71 . 1 2279 ATOM C CG GLU A 297 . −16.115 −15.553 19.320 1.00 44.97 . 1 2280 ATOM C CD GLU A 297 . −16.068 −17.055 19.141 1.00 47.13 . 1 2281 ATOM O OE1 GLU A 297 . −15.943 −17.510 17.975 1.00 49.16 . 1 2282 ATOM O OE2 GLU A 297 . −16.163 −17.775 20.164 1.00 48.98 . 1 2283 ATOM N N ASN A 298 . −18.556 −14.686 21.792 1.00 36.78 . 1 2284 ATOM C CA ASN A 298 . −18.603 −13.784 22.939 1.00 37.30 . 1 2285 ATOM C C ASN A 298 . −17.641 −12.598 22.887 1.00 36.31 . 1 2286 ATOM O O ASN A 298 . −18.013 −11.489 23.289 1.00 35.15 . 1 2287 ATOM C CB ASN A 298 . −18.366 −14.518 24.265 1.00 39.07 . 1 2288 ATOM C CG ASN A 298 . −18.377 −13.548 25.478 1.00 41.05 . 1 2289 ATOM O OD1 ASN A 298 . −17.369 −13.388 26.168 1.00 42.82 . 1 2290 ATOM N ND2 ASN A 298 . −19.530 −12.901 25.722 1.00 41.83 . 1 2291 ATOM N N GLN A 299 . −16.403 −12.798 22.431 1.00 35.25 . 1 2292 ATOM C CA GLN A 299 . −15.500 −11.660 22.388 1.00 35.16 . 1 2293 ATOM C C GLN A 299 . −16.061 −10.559 21.468 1.00 33.76 . 1 2294 ATOM O O GLN A 299 . −15.858 −9.361 21.719 1.00 32.65 . 1 2295 ATOM C CB GLN A 299 . −14.090 −12.034 21.902 1.00 37.37 . 1 2296 ATOM C CG GLN A 299 . −13.149 −10.822 21.928 1.00 41.66 . 1 2297 ATOM C CD GLN A 299 . −12.590 −10.526 23.319 1.00 44.01 . 1 2298 ATOM O OE1 GLN A 299 . −13.256 −10.748 24.343 1.00 45.36 . 1 2299 ATOM N NE2 GLN A 299 . −11.351 −10.008 23.361 1.00 44.65 . 1 2300 ATOM N N VAL A 300 . −16.755 −10.958 20.410 1.00 30.48 . 1 2301 ATOM C CA VAL A 300 . −17.310 −9.972 19.485 1.00 29.67 . 1 2302 ATOM C C VAL A 300 . −18.454 −9.248 20.163 1.00 28.46 . 1 2303 ATOM O O VAL A 300 . −18.563 −8.022 20.106 1.00 26.66 . 1 2304 ATOM C CB VAL A 300 . −17.848 −10.648 18.204 1.00 29.62 . 1 2305 ATOM C CG1 VAL A 300 . −18.548 −9.605 17.297 1.00 28.99 . 1 2306 ATOM C CG2 VAL A 300 . −16.700 −11.291 17.484 1.00 30.67 . 1 2307 ATOM N N THR A 301 . −19.301 −10.019 20.843 1.00 28.10 . 1 2308 ATOM C CA THR A 301 . −20.459 −9.420 21.547 1.00 27.31 . 1 2309 ATOM C C THR A 301 . −19.984 −8.398 22.565 1.00 27.02 . 1 2310 ATOM O O THR A 301 . −20.564 −7.265 22.730 1.00 24.41 . 1 2311 ATOM C CB THR A 301 . −21.278 −10.539 22.250 1.00 25.77 . 1 2312 ATOM O OG1 THR A 301 . −21.884 −11.355 21.235 1.00 25.73 . 1 2313 ATOM C CG2 THR A 301 . −22.323 −9.983 23.153 1.00 24.78 . 1 2314 ATOM N N GLN A 302 . −18.896 −8.767 23.221 1.00 27.15 . 1 2315 ATOM C CA GLN A 302 . −18.328 −7.880 24.224 1.00 25.18 . 1 2316 ATOM C C GLN A 302 . −17.898 −6.526 23.659 1.00 27.08 . 1 2317 ATOM O O GLN A 302 . −18.162 −5.499 24.291 1.00 25.99 . 1 2318 ATOM C CB GLN A 302 . −17.178 −8.595 24.958 1.00 27.87 . 1 2319 ATOM C CG GLN A 302 . −17.664 −9.724 25.880 1.00 29.23 . 1 2320 ATOM C CD GLN A 302 . −18.815 −9.299 26.755 1.00 30.05 . 1 2321 ATOM O OE1 GLN A 302 . −18.689 −8.336 27.515 1.00 32.99 . 1 2322 ATOM N NE2 GLN A 302 . −19.961 −10.005 26.656 1.00 28.79 . 1 2323 ATOM N N ILE A 303 . −17.262 −6.520 22.483 1.00 26.59 . 1 2324 ATOM C CA ILE A 303 . −16.820 −5.267 21.870 1.00 26.88 . 1 2325 ATOM C C ILE A 303 . −18.065 −4.490 21.413 1.00 25.35 . 1 2326 ATOM O O ILE A 303 . −18.143 −3.264 21.547 1.00 24.08 . 1 2327 ATOM C CB ILE A 303 . −15.895 −5.540 20.646 1.00 28.29 . 1 2328 ATOM C CG1 ILE A 303 . −14.549 −6.111 21.122 1.00 29.79 . 1 2329 ATOM C CG2 ILE A 303 . −15.707 −4.268 19.816 1.00 28.44 . 1 2330 ATOM C CD1 ILE A 303 . −13.839 −5.290 22.116 1.00 30.02 . 1 2331 ATOM N N LYS A 304 . −19.064 −5.194 20.884 1.00 24.11 . 1 2332 ATOM C CA LYS A 304 . −20.258 −4.453 20.433 1.00 22.50 . 1 2333 ATOM C C LYS A 304 . −20.991 −3.793 21.623 1.00 22.98 . 1 2334 ATOM O O LYS A 304 . −21.519 −2.666 21.501 1.00 22.27 . 1 2335 ATOM C CB LYS A 304 . −21.234 −5.366 19.662 1.00 22.76 . 1 2336 ATOM C CG LYS A 304 . −20.648 −5.902 18.372 1.00 20.96 . 1 2337 ATOM C CD LYS A 304 . −21.665 −6.606 17.550 1.00 23.95 . 1 2338 ATOM C CE LYS A 304 . −21.044 −7.182 16.250 1.00 24.61 . 1 2339 ATOM N NZ LYS A 304 . −21.966 −8.021 15.450 1.00 24.55 . 1 2340 ATOM N N LEU A 305 . −21.040 −4.490 22.752 1.00 21.58 . 1 2341 ATOM C CA LEU A 305 . −21.657 −3.948 23.954 1.00 21.89 . 1 2342 ATOM C C LEU A 305 . −20.882 −2.734 24.480 1.00 21.91 . 1 2343 ATOM O O LEU A 305 . −21.463 −1.767 24.996 1.00 21.53 . 1 2344 ATOM C CB LEU A 305 . −21.718 −5.021 25.033 1.00 20.60 . 1 2345 ATOM C CG LEU A 305 . −22.706 −6.141 24.757 1.00 22.74 . 1 2346 ATOM C CD1 LEU A 305 . −22.405 −7.337 25.692 1.00 24.49 . 1 2347 ATOM C CD2 LEU A 305 . −24.119 −5.611 24.935 1.00 24.42 . 1 2348 ATOM N N LEU A 306 . −19.564 −2.798 24.312 1.00 22.30 . 1 2349 ATOM C CA LEU A 306 . −18.669 −1.724 24.683 1.00 22.59 . 1 2350 ATOM C C LEU A 306 . −18.889 −0.531 23.736 1.00 22.64 . 1 2351 ATOM O O LEU A 306 . −18.935 0.625 24.185 1.00 21.72 . 1 2352 ATOM C CB LEU A 306 . −17.221 −2.215 24.621 1.00 25.61 . 1 2353 ATOM C CG LEU A 306 . −16.115 −1.160 24.715 1.00 26.10 . 1 2354 ATOM C CD1 LEU A 306 . −16.181 −0.305 26.012 1.00 26.74 . 1 2355 ATOM C CD2 LEU A 306 . −14.756 −1.917 24.644 1.00 26.09 . 1 2356 HETA N N MSE A 307 . −19.013 −0.791 22.427 1.00 23.75 . 1 2357 HETA C CA MSE A 307 . −19.268 0.319 21.519 1.00 24.69 . 1 2358 HETA C C MSE A 307 . −20.605 0.938 21.885 1.00 23.84 . 1 2359 HETA O O MSE A 307 . −20.794 2.173 21.766 1.00 22.31 . 1 2360 HETA C CB MSE A 307 . −19.295 −0.146 20.044 1.00 27.51 . 1 2361 HETA C CG MSE A 307 . −17.954 −0.715 19.547 1.00 28.76 . 1 2362 HETA SE SE MSE A 307 . −16.633 0.561 19.696 1.00 34.47 . 1 2363 HETA C CE MSE A 307 . −17.670 2.152 19.036 1.00 18.44 . 1 2364 ATOM N N ASP A 308 . −21.570 0.126 22.327 1.00 22.62 . 1 2365 ATOM C CA ASP A 308 . −22.889 0.684 22.663 1.00 22.60 . 1 2366 ATOM C C ASP A 308 . −22.765 1.668 23.822 1.00 21.41 . 1 2367 ATOM O O ASP A 308 . −23.324 2.771 23.838 1.00 19.83 . 1 2368 ATOM C CB ASP A 308 . −23.881 −0.443 22.998 1.00 22.26 . 1 2369 ATOM C CG ASP A 308 . −25.205 0.084 23.499 1.00 22.42 . 1 2370 ATOM O OD1 ASP A 308 . −25.930 0.726 22.711 1.00 23.18 . 1 2371 ATOM O OD2 ASP A 308 . −25.534 −0.129 24.678 1.00 23.24 . 1 2372 ATOM N N VAL A 309 . −21.963 1.275 24.790 1.00 21.46 . 1 2373 ATOM C CA VAL A 309 . −21.805 2.178 25.918 1.00 21.49 . 1 2374 ATOM C C VAL A 309 . −21.087 3.444 25.451 1.00 22.43 . 1 2375 ATOM O O VAL A 309 . −21.420 4.601 25.853 1.00 21.16 . 1 2376 ATOM C CB VAL A 309 . −21.021 1.463 27.064 1.00 20.98 . 1 2377 ATOM C CG1 VAL A 309 . −20.529 2.502 28.060 1.00 22.45 . 1 2378 ATOM C CG2 VAL A 309 . −21.924 0.433 27.769 1.00 23.57 . 1 2379 ATOM N N ASN A 310 . −20.086 3.247 24.595 1.00 21.13 . 1 2380 ATOM C CA ASN A 310 . −19.313 4.375 24.116 1.00 21.70 . 1 2381 ATOM C C ASN A 310 . −20.173 5.389 23.374 1.00 21.50 . 1 2382 ATOM O O ASN A 310 . −19.852 6.563 23.364 1.00 19.60 . 1 2383 ATOM C CB ASN A 310 . −18.171 3.854 23.232 1.00 23.01 . 1 2384 ATOM C CG ASN A 310 . −17.437 4.964 22.480 1.00 23.54 . 1 2385 ATOM O OD1 ASN A 310 . −17.545 5.113 21.253 1.00 27.20 . 1 2386 ATOM N ND2 ASN A 310 . −16.661 5.729 23.204 1.00 22.57 . 1 2387 HETA N N MSE A 311 . −21.308 4.938 22.811 1.00 20.99 . 1 2388 HETA C CA MSE A 311 . −22.129 5.851 22.032 1.00 20.59 . 1 2389 HETA C C MSE A 311 . −22.894 6.914 22.849 1.00 22.15 . 1 2390 HETA O O MSE A 311 . −23.647 7.699 22.297 1.00 22.36 . 1 2391 HETA C CB MSE A 311 . −23.072 5.061 21.114 1.00 20.76 . 1 2392 HETA C CG MSE A 311 . −22.389 4.373 19.926 1.00 23.01 . 1 2393 HETA SE SE MSE A 311 . −21.104 5.422 18.955 1.00 19.07 . 1 2394 HETA C CE MSE A 311 . −22.258 6.819 18.488 1.00 25.01 . 1 2395 ATOM N N ALA A 312 . −22.671 6.944 24.170 1.00 22.32 . 1 2396 ATOM C CA ALA A 312 . −23.293 7.957 24.995 1.00 22.05 . 1 2397 ATOM C C ALA A 312 . −22.869 9.310 24.437 1.00 21.18 . 1 2398 ATOM O O ALA A 312 . −23.552 10.318 24.599 1.00 22.10 . 1 2399 ATOM C CB ALA A 312 . −22.815 7.796 26.492 1.00 21.80 . 1 2400 ATOM N N CYS A 313 . −21.686 9.369 23.837 1.00 22.10 . 1 2401 ATOM C CA CYS A 313 . −21.208 10.625 23.245 1.00 21.76 . 1 2402 ATOM C C CYS A 313 . −22.294 11.356 22.409 1.00 21.77 . 1 2403 ATOM O O CYS A 313 . −22.386 12.616 22.445 1.00 20.31 . 1 2404 ATOM C CB CYS A 313 . −19.968 10.361 22.361 1.00 22.27 . 1 2405 ATOM S SG CYS A 313 . −20.200 9.193 20.943 1.00 22.42 . 1 2406 ATOM N N LEU A 314 . −23.094 10.606 21.650 1.00 20.33 . 1 2407 ATOM C CA LEU A 314 . −24.185 11.218 20.826 1.00 20.69 . 1 2408 ATOM C C LEU A 314 . −25.590 10.675 21.195 1.00 22.62 . 1 2409 ATOM O O LEU A 314 . −26.545 10.784 20.376 1.00 21.49 . 1 2410 ATOM C CB LEU A 314 . −23.922 10.934 19.318 1.00 21.33 . 1 2411 ATOM C CG LEU A 314 . −22.540 11.197 18.762 1.00 23.31 . 1 2412 ATOM C CD1 LEU A 314 . −22.470 10.895 17.249 1.00 23.71 . 1 2413 ATOM C CD2 LEU A 314 . −22.187 12.654 19.012 1.00 25.02 . 1 2414 ATOM N N ASN A 315 . −25.754 10.127 22.406 1.00 21.00 . 1 2415 ATOM C CA ASN A 315 . −27.013 9.453 22.770 1.00 21.34 . 1 2416 ATOM C C ASN A 315 . −27.341 8.372 21.716 1.00 19.73 . 1 2417 ATOM O O ASN A 315 . −28.506 8.120 21.421 1.00 20.03 . 1 2418 ATOM C CB ASN A 315 . −28.216 10.390 22.844 1.00 20.94 . 1 2419 ATOM C CG ASN A 315 . −28.129 11.328 24.029 1.00 24.52 . 1 2420 ATOM O OD1 ASN A 315 . −28.792 12.379 24.065 1.00 27.10 . 1 2421 ATOM N ND2 ASN A 315 . −27.300 10.972 24.990 1.00 20.06 . 1 2422 ATOM N N GLY A 316 . −26.293 7.810 21.128 1.00 20.64 . 1 2423 ATOM C CA GLY A 316 . −26.437 6.795 20.104 1.00 19.58 . 1 2424 ATOM C C GLY A 316 . −26.586 5.422 20.710 1.00 20.12 . 1 2425 ATOM O O GLY A 316 . −26.698 5.286 21.952 1.00 22.13 . 1 2426 ATOM N N LYS A 317 . −26.549 4.374 19.873 1.00 20.56 . 1 2427 ATOM C CA LYS A 317 . −26.810 3.030 20.374 1.00 21.01 . 1 2428 ATOM C C LYS A 317 . −26.382 2.026 19.351 1.00 22.11 . 1 2429 ATOM O O LYS A 317 . −26.353 2.338 18.159 1.00 21.38 . 1 2430 ATOM C CB LYS A 317 . −28.339 2.891 20.634 1.00 25.45 . 1 2431 ATOM C CG LYS A 317 . −28.841 1.551 21.245 1.00 25.41 . 1 2432 ATOM C CD LYS A 317 . −30.371 1.442 21.249 1.00 26.63 . 1 2433 ATOM C CE LYS A 317 . −31.011 2.452 22.162 1.00 27.24 . 1 2434 ATOM N NZ LYS A 317 . −32.555 2.424 22.150 1.00 30.46 . 1 2435 ATOM N N GLU A 318 . −26.001 0.836 19.809 1.00 21.42 . 1 2436 ATOM C CA GLU A 318 . −25.657 −0.241 18.881 1.00 23.01 . 1 2437 ATOM C C GLU A 318 . −26.790 −1.186 19.201 1.00 22.35 . 1 2438 ATOM O O GLU A 318 . −26.980 −1.638 20.351 1.00 24.09 . 1 2439 ATOM C CB GLU A 318 . −24.269 −0.833 19.170 1.00 21.85 . 1 2440 ATOM C CG GLU A 318 . −23.120 0.177 18.939 1.00 23.44 . 1 2441 ATOM C CD GLU A 318 . −22.960 0.779 17.530 1.00 22.98 . 1 2442 ATOM O OE1 GLU A 318 . −23.623 0.386 16.546 1.00 22.09 . 1 2443 ATOM O OE2 GLU A 318 . −22.092 1.684 17.422 1.00 23.21 . 1 2444 ATOM N N ARG A 319 . −27.572 −1.445 18.171 1.00 22.62 . 1 2445 ATOM C CA ARG A 319 . −28.803 −2.188 18.292 1.00 20.51 . 1 2446 ATOM C C ARG A 319 . −28.806 −3.676 17.967 1.00 21.64 . 1 2447 ATOM O O ARG A 319 . −28.116 −4.114 17.055 1.00 21.25 . 1 2448 ATOM C CB ARG A 319 . −29.867 −1.485 17.420 1.00 19.98 . 1 2449 ATOM C CG ARG A 319 . −30.198 −0.033 17.858 1.00 23.47 . 1 2450 ATOM C CD ARG A 319 . −31.134 0.703 16.915 1.00 21.18 . 1 2451 ATOM N NE ARG A 319 . −31.531 2.013 17.473 1.00 20.52 . 1 2452 ATOM C CZ ARG A 319 . −30.886 3.171 17.352 1.00 21.20 . 1 2453 ATOM N NH1 ARG A 319 . −29.747 3.294 16.643 1.00 20.86 . 1 2454 ATOM N NH2 ARG A 319 . −31.352 4.234 18.040 1.00 20.54 . 1 2455 ATOM N N ASN A 320 . −29.618 −4.413 18.720 1.00 23.42 . 1 2456 ATOM C CA ASN A 320 . −29.771 −5.808 18.437 1.00 23.06 . 1 2457 ATOM C C ASN A 320 . −30.907 −5.904 17.414 1.00 23.03 . 1 2458 ATOM O O ASN A 320 . −31.516 −4.870 17.044 1.00 22.35 . 1 2459 ATOM C CB ASN A 320 . −30.042 −6.619 19.721 1.00 23.53 . 1 2460 ATOM C CG ASN A 320 . −31.367 −6.282 20.397 1.00 23.29 . 1 2461 ATOM O OD1 ASN A 320 . −32.350 −5.900 19.764 1.00 25.55 . 1 2462 ATOM N ND2 ASN A 320 . −31.405 −6.467 21.728 1.00 26.90 . 1 2463 ATOM N N GLU A 321 . −31.203 −7.120 16.936 1.00 23.91 . 1 2464 ATOM C CA GLU A 321 . −32.248 −7.241 15.901 1.00 24.98 . 1 2465 ATOM C C GLU A 321 . −33.629 −6.838 16.320 1.00 25.87 . 1 2466 ATOM O O GLU A 321 . −34.325 −6.231 15.537 1.00 26.56 . 1 2467 ATOM C CB GLU A 321 . −32.291 −8.658 15.294 1.00 26.81 . 1 2468 ATOM C CG GLU A 321 . −33.433 −8.855 14.240 1.00 27.49 . 1 2469 ATOM C CD GLU A 321 . −33.306 −10.198 13.498 1.00 29.84 . 1 2470 ATOM O OE1 GLU A 321 . −32.395 −10.992 13.875 1.00 30.79 . 1 2471 ATOM O OE2 GLU A 321 . −34.094 −10.440 12.548 1.00 28.17 . 1 2472 ATOM N N GLU A 322 . −34.043 −7.129 17.547 1.00 26.72 . 1 2473 ATOM C CA GLU A 322 . −35.388 −6.715 17.942 1.00 28.47 . 1 2474 ATOM C C GLU A 322 . −35.489 −5.214 17.989 1.00 26.69 . 1 2475 ATOM O O GLU A 322 . −36.530 −4.682 17.662 1.00 25.71 . 1 2476 ATOM C CB GLU A 322 . −35.795 −7.353 19.267 1.00 32.08 . 1 2477 ATOM C CG GLU A 322 . −36.068 −8.867 19.084 1.00 36.73 . 1 2478 ATOM C CD GLU A 322 . −37.300 −9.185 18.184 1.00 39.51 . 1 2479 ATOM O OE1 GLU A 322 . −37.263 −10.217 17.460 1.00 41.34 . 1 2480 ATOM O OE2 GLU A 322 . −38.311 −8.424 18.206 1.00 41.90 . 1 2481 ATOM N N GLU A 323 . −34.383 −4.549 18.368 1.00 25.73 . 1 2482 ATOM C CA GLU A 323 . −34.382 −3.073 18.436 1.00 23.92 . 1 2483 ATOM C C GLU A 323 . −34.457 −2.501 17.026 1.00 24.35 . 1 2484 ATOM O O GLU A 323 . −35.199 −1.530 16.776 1.00 25.59 . 1 2485 ATOM C CB GLU A 323 . −33.129 −2.533 19.166 1.00 23.08 . 1 2486 ATOM C CG GLU A 323 . −33.218 −2.856 20.656 1.00 24.03 . 1 2487 ATOM C CD GLU A 323 . −31.952 −2.562 21.397 1.00 25.06 . 1 2488 ATOM O OE1 GLU A 323 . −30.861 −2.772 20.860 1.00 24.53 . 1 2489 ATOM O OE2 GLU A 323 . −32.049 −2.115 22.555 1.00 28.95 . 1 2490 ATOM N N TRP A 324 . −33.705 −3.087 16.102 1.00 24.62 . 1 2491 ATOM C CA TRP A 324 . −33.761 −2.612 14.722 1.00 23.09 . 1 2492 ATOM C C TRP A 324 . −35.175 −2.821 14.183 1.00 24.71 . 1 2493 ATOM O O TRP A 324 . −35.781 −1.924 13.612 1.00 23.64 . 1 2494 ATOM C CB TRP A 324 . −32.766 −3.370 13.854 1.00 23.72 . 1 2495 ATOM C CG TRP A 324 . −31.354 −2.900 14.008 1.00 22.04 . 1 2496 ATOM C CD1 TRP A 324 . −30.266 −3.631 14.423 1.00 22.49 . 1 2497 ATOM C CD2 TRP A 324 . −30.832 −1.618 13.601 1.00 20.57 . 1 2498 ATOM N NE1 TRP A 324 . −29.125 −2.897 14.275 1.00 20.99 . 1 2499 ATOM C CE2 TRP A 324 . −29.440 −1.662 13.767 1.00 20.70 . 1 2500 ATOM C CE3 TRP A 324 . −31.417 −0.455 13.096 1.00 21.87 . 1 2501 ATOM C CZ2 TRP A 324 . −28.603 −0.579 13.438 1.00 20.06 . 1 2502 ATOM C CZ3 TRP A 324 . −30.588 0.630 12.767 1.00 20.95 . 1 2503 ATOM C CH2 TRP A 324 . −29.195 0.554 12.939 1.00 20.36 . 1 2504 ATOM N N LYS A 325 . −35.679 −4.036 14.351 1.00 24.68 . 1 2505 ATOM C CA LYS A 325 . −37.021 −4.344 13.859 1.00 27.62 . 1 2506 ATOM C C LYS A 325 . −38.105 −3.398 14.363 1.00 28.29 . 1 2507 ATOM O O LYS A 325 . −38.968 −2.966 13.602 1.00 28.37 . 1 2508 ATOM C CB LYS A 325 . −37.354 −5.774 14.205 1.00 28.31 . 1 2509 ATOM C CG LYS A 325 . −38.708 −6.245 13.665 1.00 30.59 . 1 2510 ATOM C CD LYS A 325 . −38.988 −7.609 14.227 1.00 32.18 . 1 2511 ATOM C CE LYS A 325 . −40.356 −8.142 13.843 1.00 35.47 . 1 2512 ATOM N NZ LYS A 325 . −40.634 −9.380 14.674 1.00 37.83 . 1 2513 ATOM N N LYS A 326 . −38.038 −3.007 15.631 1.00 27.91 . 1 2514 ATOM C CA LYS A 326 . −39.026 −2.123 16.206 1.00 27.71 . 1 2515 ATOM C C LYS A 326 . −38.991 −0.747 15.532 1.00 26.43 . 1 2516 ATOM O O LYS A 326 . −40.038 −0.109 15.350 1.00 25.87 . 1 2517 ATOM C CB LYS A 326 . −38.750 −2.005 17.713 1.00 30.09 . 1 2518 ATOM C CG LYS A 326 . −39.862 −1.438 18.567 1.00 33.62 . 1 2519 ATOM C CD LYS A 326 . −39.404 −1.281 20.024 1.00 36.26 . 1 2520 ATOM C CE LYS A 326 . −40.563 −0.875 20.941 1.00 38.31 . 1 2521 ATOM N NZ LYS A 326 . −41.139 0.455 20.571 1.00 41.37 . 1 2522 ATOM N N LEU A 327 . −37.796 −0.283 15.172 1.00 25.54 . 1 2523 ATOM C CA LEU A 327 . −37.691 1.027 14.528 1.00 24.93 . 1 2524 ATOM C C LEU A 327 . −38.262 0.901 13.143 1.00 24.61 . 1 2525 ATOM O O LEU A 327 . −39.057 1.735 12.707 1.00 24.79 . 1 2526 ATOM C CB LEU A 327 . −36.238 1.509 14.402 1.00 24.94 . 1 2527 ATOM C CG LEU A 327 . −35.562 2.004 15.656 1.00 27.97 . 1 2528 ATOM C CD1 LEU A 327 . −34.065 2.198 15.407 1.00 28.05 . 1 2529 ATOM C CD2 LEU A 327 . −36.210 3.307 16.038 1.00 26.91 . 1 2530 ATOM N N PHE A 328 . −37.878 −0.157 12.455 1.00 23.31 . 1 2531 ATOM C CA PHE A 328 . −38.370 −0.335 11.074 1.00 23.65 . 1 2532 ATOM C C PHE A 328 . −39.895 −0.330 11.036 1.00 24.38 . 1 2533 ATOM O O PHE A 328 . −40.497 0.338 10.187 1.00 24.75 . 1 2534 ATOM C CB PHE A 328 . −37.788 −1.631 10.476 1.00 22.27 . 1 2535 ATOM C CG PHE A 328 . −36.268 −1.653 10.379 1.00 20.37 . 1 2536 ATOM C CD1 PHE A 328 . −35.590 −2.876 10.367 1.00 20.94 . 1 2537 ATOM C CD2 PHE A 328 . −35.513 −0.476 10.413 1.00 21.08 . 1 2538 ATOM C CE1 PHE A 328 . −34.189 −2.928 10.406 1.00 21.64 . 1 2539 ATOM C CE2 PHE A 328 . −34.108 −0.521 10.453 1.00 19.76 . 1 2540 ATOM C CZ PHE A 328 . −33.456 −1.746 10.454 1.00 21.64 . 1 2541 ATOM N N ILE A 329 . −40.534 −1.047 11.955 1.00 26.04 . 1 2542 ATOM C CA ILE A 329 . −41.990 −1.132 11.989 1.00 27.18 . 1 2543 ATOM C C ILE A 329 . −42.628 0.229 12.329 1.00 27.80 . 1 2544 ATOM O O ILE A 329 . −43.586 0.638 11.650 1.00 27.92 . 1 2545 ATOM C CB ILE A 329 . −42.443 −2.274 12.944 1.00 27.80 . 1 2546 ATOM C CG1 ILE A 329 . −42.003 −3.613 12.326 1.00 29.47 . 1 2547 ATOM C CG2 ILE A 329 . −43.985 −2.321 13.060 1.00 31.04 . 1 2548 ATOM C CD1 ILE A 329 . −42.106 −4.820 13.293 1.00 28.00 . 1 2549 ATOM N N GLU A 330 . −42.063 0.957 13.301 1.00 27.36 . 1 2550 ATOM C CA GLU A 330 . −42.611 2.265 13.678 1.00 29.23 . 1 2551 ATOM C C GLU A 330 . −42.435 3.281 12.549 1.00 28.43 . 1 2552 ATOM O O GLU A 330 . −43.329 4.113 12.311 1.00 28.83 . 1 2553 ATOM C CB GLU A 330 . −41.985 2.759 15.000 1.00 28.57 . 1 2554 ATOM C CG GLU A 330 . −42.529 4.100 15.475 1.00 35.66 . 1 2555 ATOM C CD GLU A 330 . −42.439 4.289 16.999 1.00 37.88 . 1 2556 ATOM O OE1 GLU A 330 . −41.539 3.695 17.636 1.00 40.09 . 1 2557 ATOM O OE2 GLU A 330 . −43.271 5.061 17.548 1.00 42.00 . 1 2558 ATOM N N ALA A 331 . −41.327 3.173 11.808 1.00 27.05 . 1 2559 ATOM C CA ALA A 331 . −41.037 4.053 10.678 1.00 26.45 . 1 2560 ATOM C C ALA A 331 . −41.873 3.649 9.421 1.00 26.23 . 1 2561 ATOM O O ALA A 331 . −41.777 4.285 8.353 1.00 28.12 . 1 2562 ATOM C CB ALA A 331 . −39.546 4.032 10.382 1.00 26.72 . 1 2563 ATOM N N GLY A 332 . −42.675 2.598 9.555 1.00 26.41 . 1 2564 ATOM C CA GLY A 332 . −43.543 2.163 8.456 1.00 28.35 . 1 2565 ATOM C C GLY A 332 . −42.999 1.291 7.319 1.00 27.72 . 1 2566 ATOM O O GLY A 332 . −43.553 1.286 6.214 1.00 30.21 . 1 2567 ATOM N N PHE A 333 . −41.881 0.612 7.543 1.00 25.23 . 1 2568 ATOM C CA PHE A 333 . −41.367 −0.286 6.545 1.00 24.18 . 1 2569 ATOM C C PHE A 333 . −42.057 −1.624 6.712 1.00 23.98 . 1 2570 ATOM O O PHE A 333 . −42.429 −2.001 7.826 1.00 25.40 . 1 2571 ATOM C CB PHE A 333 . −39.861 −0.404 6.680 1.00 23.62 . 1 2572 ATOM C CG PHE A 333 . −39.166 0.852 6.293 1.00 21.20 . 1 2573 ATOM C CD1 PHE A 333 . −39.133 1.931 7.165 1.00 22.46 . 1 2574 ATOM C CD2 PHE A 333 . −38.583 0.986 5.014 1.00 20.37 . 1 2575 ATOM C CE1 PHE A 333 . −38.507 3.122 6.752 1.00 23.25 . 1 2576 ATOM C CE2 PHE A 333 . −37.973 2.139 4.606 1.00 24.14 . 1 2577 ATOM C CZ PHE A 333 . −37.913 3.233 5.466 1.00 22.66 . 1 2578 ATOM N N GLN A 334 . −42.208 −2.350 5.614 1.00 23.42 . 1 2579 ATOM C CA GLN A 334 . −42.920 −3.640 5.637 1.00 23.56 . 1 2580 ATOM C C GLN A 334 . −42.125 −4.864 6.036 1.00 23.75 . 1 2581 ATOM O O GLN A 334 . −42.685 −5.807 6.609 1.00 24.45 . 1 2582 ATOM C CB GLN A 334 . −43.610 −3.921 4.294 1.00 23.15 . 1 2583 ATOM C CG GLN A 334 . −44.610 −2.818 3.884 1.00 25.72 . 1 2584 ATOM C CD GLN A 334 . −45.383 −3.174 2.629 1.00 26.87 . 1 2585 ATOM O OE1 GLN A 334 . −45.034 −2.743 1.509 1.00 27.77 . 1 2586 ATOM N NE2 GLN A 334 . −46.425 −3.992 2.796 1.00 23.80 . 1 2587 ATOM N N HIS A 335 . −40.848 −4.891 5.709 1.00 23.79 . 1 2588 ATOM C CA HIS A 335 . −40.041 −6.052 6.080 1.00 23.37 . 1 2589 ATOM C C HIS A 335 . −38.585 −5.676 5.916 1.00 23.06 . 1 2590 ATOM O O HIS A 335 . −38.249 −4.672 5.290 1.00 23.62 . 1 2591 ATOM C CB HIS A 335 . −40.409 −7.283 5.211 1.00 25.40 . 1 2592 ATOM C CG HIS A 335 . −40.101 −7.135 3.742 1.00 24.56 . 1 2593 ATOM N ND1 HIS A 335 . −39.060 −7.805 3.128 1.00 24.78 . 1 2594 ATOM C CD2 HIS A 335 . −40.770 −6.502 2.752 1.00 25.07 . 1 2595 ATOM C CE1 HIS A 335 . −39.105 −7.593 1.828 1.00 23.83 . 1 2596 ATOM N NE2 HIS A 335 . −40.142 −6.812 1.572 1.00 24.73 . 1 2597 ATOM N N TYR A 336 . −37.712 −6.483 6.478 1.00 23.14 . 1 2598 ATOM C CA TYR A 336 . −36.296 −6.191 6.422 1.00 24.07 . 1 2599 ATOM C C TYR A 336 . −35.457 −7.443 6.304 1.00 23.36 . 1 2600 ATOM O O TYR A 336 . −35.932 −8.554 6.540 1.00 25.34 . 1 2601 ATOM C CB TYR A 336 . −35.895 −5.428 7.695 1.00 23.40 . 1 2602 ATOM C CG TYR A 336 . −35.944 −6.286 8.971 1.00 22.83 . 1 2603 ATOM C CD1 TYR A 336 . −34.827 −7.004 9.414 1.00 23.24 . 1 2604 ATOM C CD2 TYR A 336 . −37.148 −6.422 9.679 1.00 24.26 . 1 2605 ATOM C CE1 TYR A 336 . −34.898 −7.845 10.528 1.00 24.31 . 1 2606 ATOM C CE2 TYR A 336 . −37.246 −7.271 10.810 1.00 25.66 . 1 2607 ATOM C CZ TYR A 336 . −36.138 −7.974 11.221 1.00 25.81 . 1 2608 ATOM O OH TYR A 336 . −36.341 −8.807 12.310 1.00 27.32 . 1 2609 ATOM N N LYS A 337 . −34.197 −7.258 5.977 1.00 23.83 . 1 2610 ATOM C CA LYS A 337 . −33.257 −8.345 5.842 1.00 23.09 . 1 2611 ATOM C C LYS A 337 . −31.909 −7.914 6.381 1.00 24.85 . 1 2612 ATOM O O LYS A 337 . −31.449 −6.818 6.068 1.00 25.32 . 1 2613 ATOM C CB LYS A 337 . −33.120 −8.765 4.396 1.00 22.37 . 1 2614 ATOM C CG LYS A 337 . −34.440 −9.309 3.786 1.00 22.19 . 1 2615 ATOM C CD LYS A 337 . −34.256 −9.723 2.357 1.00 25.04 . 1 2616 ATOM C CE LYS A 337 . −35.569 −10.277 1.753 1.00 23.48 . 1 2617 ATOM N NZ LYS A 337 . −35.249 −11.008 0.486 1.00 25.84 . 1 2618 ATOM N N ILE A 338 . −31.318 −8.773 7.210 1.00 23.48 . 1 2619 ATOM C CA ILE A 338 . −29.981 −8.551 7.755 1.00 24.63 . 1 2620 ATOM C C ILE A 338 . −29.014 −9.618 7.206 1.00 24.95 . 1 2621 ATOM O O ILE A 338 . −29.336 −10.828 7.194 1.00 26.89 . 1 2622 ATOM C CB ILE A 338 . −29.972 −8.609 9.313 1.00 24.26 . 1 2623 ATOM C CG1 ILE A 338 . −30.942 −7.550 9.900 1.00 22.24 . 1 2624 ATOM C CG2 ILE A 338 . −28.525 −8.473 9.796 1.00 23.31 . 1 2625 ATOM C CD1 ILE A 338 . −31.165 −7.569 11.436 1.00 24.72 . 1 2626 ATOM N N SER A 339 . −27.860 −9.159 6.716 1.00 25.31 . 1 2627 ATOM C CA SER A 339 . −26.786 −10.000 6.199 1.00 26.77 . 1 2628 ATOM C C SER A 339 . −25.463 −9.565 6.819 1.00 26.63 . 1 2629 ATOM O O SER A 339 . −25.272 −8.391 7.132 1.00 23.33 . 1 2630 ATOM C CB SER A 339 . −26.696 −9.865 4.677 1.00 29.71 . 1 2631 ATOM O OG SER A 339 . −27.991 −10.076 4.070 1.00 34.03 . 1 2632 ATOM N N PRO A 340 . −24.515 −10.495 7.025 1.00 27.66 . 1 2633 ATOM C CA PRO A 340 . −23.277 −9.984 7.607 1.00 27.44 . 1 2634 ATOM C C PRO A 340 . −22.507 −9.290 6.504 1.00 26.71 . 1 2635 ATOM O O PRO A 340 . −22.629 −9.664 5.353 1.00 27.03 . 1 2636 ATOM C CB PRO A 340 . −22.583 −11.239 8.101 1.00 28.65 . 1 2637 ATOM C CG PRO A 340 . −23.063 −12.267 7.183 1.00 28.94 . 1 2638 ATOM C CD PRO A 340 . −24.517 −11.965 6.997 1.00 29.46 . 1 2639 ATOM N N LEU A 341 . −21.733 −8.268 6.828 1.00 25.28 . 1 2640 ATOM C CA LEU A 341 . −20.985 −7.575 5.782 1.00 24.58 . 1 2641 ATOM C C LEU A 341 . −19.467 −7.731 5.928 1.00 25.34 . 1 2642 ATOM O O LEU A 341 . −18.785 −8.228 5.037 1.00 25.27 . 1 2643 ATOM C CB LEU A 341 . −21.374 −6.066 5.764 1.00 24.62 . 1 2644 ATOM C CG LEU A 341 . −20.724 −5.221 4.697 1.00 23.68 . 1 2645 ATOM C CD1 LEU A 341 . −21.149 −5.638 3.304 1.00 22.12 . 1 2646 ATOM C CD2 LEU A 341 . −21.041 −3.781 4.946 1.00 22.61 . 1 2647 ATOM N N THR A 342 . −18.923 −7.291 7.043 1.00 26.21 . 1 2648 ATOM C CA THR A 342 . −17.470 −7.432 7.260 1.00 27.27 . 1 2649 ATOM C C THR A 342 . −17.168 −7.106 8.706 1.00 26.04 . 1 2650 ATOM O O THR A 342 . −17.684 −6.123 9.237 1.00 23.61 . 1 2651 ATOM C CB THR A 342 . −16.591 −6.483 6.325 1.00 27.33 . 1 2652 ATOM O OG1 THR A 342 . −15.208 −6.654 6.664 1.00 29.78 . 1 2653 ATOM C CG2 THR A 342 . −16.912 −4.988 6.558 1.00 28.50 . 1 2654 ATOM N N GLY A 343 . −16.356 −7.962 9.356 1.00 26.25 . 1 2655 ATOM C CA GLY A 343 . −16.002 −7.755 10.742 1.00 25.93 . 1 2656 ATOM C C GLY A 343 . −17.199 −7.528 11.663 1.00 26.21 . 1 2657 ATOM O O GLY A 343 . −18.082 −8.372 11.812 1.00 24.32 . 1 2658 ATOM N N PHE A 344 . −17.199 −6.371 12.309 1.00 26.17 . 1 2659 ATOM C CA PHE A 344 . −18.249 −6.036 13.246 1.00 24.97 . 1 2660 ATOM C C PHE A 344 . −19.556 −5.582 12.569 1.00 24.65 . 1 2661 ATOM O O PHE A 344 . −20.588 −5.521 13.251 1.00 22.16 . 1 2662 ATOM C CB PHE A 344 . −17.798 −4.884 14.155 1.00 28.27 . 1 2663 ATOM C CG PHE A 344 . −16.723 −5.258 15.158 1.00 29.62 . 1 2664 ATOM C CD1 PHE A 344 . −15.405 −4.857 14.964 1.00 31.83 . 1 2665 ATOM C CD2 PHE A 344 . −17.018 −6.043 16.256 1.00 30.79 . 1 2666 ATOM C CE1 PHE A 344 . −14.404 −5.249 15.857 1.00 31.76 . 1 2667 ATOM C CE2 PHE A 344 . −16.010 −6.441 17.156 1.00 31.15 . 1 2668 ATOM C CZ PHE A 344 . −14.711 −6.038 16.944 1.00 32.83 . 1 2669 ATOM N N LEU A 345 . −19.518 −5.280 11.268 1.00 22.75 . 1 2670 ATOM C CA LEU A 345 . −20.726 −4.723 10.637 1.00 23.72 . 1 2671 ATOM C C LEU A 345 . −21.640 −5.656 9.857 1.00 23.38 . 1 2672 ATOM O O LEU A 345 . −21.191 −6.665 9.294 1.00 23.27 . 1 2673 ATOM C CB LEU A 345 . −20.300 −3.550 9.733 1.00 24.06 . 1 2674 ATOM C CG LEU A 345 . −19.454 −2.473 10.448 1.00 25.26 . 1 2675 ATOM C CD1 LEU A 345 . −18.905 −1.482 9.423 1.00 25.55 . 1 2676 ATOM C CD2 LEU A 345 . −20.290 −1.753 11.489 1.00 27.63 . 1 2677 ATOM N N SER A 346 . −22.924 −5.293 9.826 1.00 22.66 . 1 2678 ATOM C CA SER A 346 . −23.943 −6.038 9.061 1.00 23.39 . 1 2679 ATOM C C SER A 346 . −24.503 −5.146 7.988 1.00 23.61 . 1 2680 ATOM O O SER A 346 . −24.348 −3.909 8.053 1.00 22.56 . 1 2681 ATOM C CB SER A 346 . −25.103 −6.460 9.959 1.00 25.44 . 1 2682 ATOM O OG SER A 346 . −24.685 −7.349 11.010 1.00 24.37 . 1 2683 ATOM N N LEU A 347 . −25.208 −5.748 7.026 1.00 22.93 . 1 2684 ATOM C CA LEU A 347 . −25.848 −4.953 5.983 1.00 21.78 . 1 2685 ATOM C C LEU A 347 . −27.335 −5.184 6.211 1.00 22.42 . 1 2686 ATOM O O LEU A 347 . −27.802 −6.318 6.191 1.00 23.23 . 1 2687 ATOM C CB LEU A 347 . −25.406 −5.441 4.584 1.00 23.52 . 1 2688 ATOM C CG LEU A 347 . −25.865 −4.725 3.318 1.00 23.98 . 1 2689 ATOM C CD1 LEU A 347 . −27.354 −4.682 3.378 1.00 27.45 . 1 2690 ATOM C CD2 LEU A 347 . −25.278 −3.301 3.196 1.00 26.17 . 1 2691 ATOM N N ILE A 348 . −28.098 −4.122 6.386 1.00 20.49 . 1 2692 ATOM C CA ILE A 348 . −29.519 −4.326 6.633 1.00 22.16 . 1 2693 ATOM C C ILE A 348 . −30.282 −3.630 5.494 1.00 22.54 . 1 2694 ATOM O O ILE A 348 . −29.917 −2.522 5.094 1.00 22.00 . 1 2695 ATOM C CB ILE A 348 . −29.964 −3.677 7.987 1.00 21.59 . 1 2696 ATOM C CG1 ILE A 348 . −29.178 −4.248 9.166 1.00 23.49 . 1 2697 ATOM C CG2 ILE A 348 . −31.469 −3.951 8.212 1.00 23.60 . 1 2698 ATOM C CD1 ILE A 348 . −29.551 −3.568 10.493 1.00 25.55 . 1 2699 ATOM N N GLU A 349 . −31.304 −4.294 4.925 1.00 22.73 . 1 2700 ATOM C CA GLU A 349 . −32.056 −3.622 3.856 1.00 23.31 . 1 2701 ATOM C C GLU A 349 . −33.501 −3.574 4.347 1.00 23.59 . 1 2702 ATOM O O GLU A 349 . −33.995 −4.546 4.940 1.00 23.24 . 1 2703 ATOM C CB GLU A 349 . −31.915 −4.387 2.509 1.00 25.52 . 1 2704 ATOM C CG GLU A 349 . −30.477 −4.338 1.997 1.00 26.69 . 1 2705 ATOM C CD GLU A 349 . −30.332 −4.340 0.497 1.00 30.24 . 1 2706 ATOM O OE1 GLU A 349 . −30.345 −5.436 −0.099 1.00 33.91 . 1 2707 ATOM O OE2 GLU A 349 . −30.203 −3.261 −0.105 1.00 30.47 . 1 2708 ATOM N N ILE A 350 . −34.153 −2.426 4.221 1.00 19.97 . 1 2709 ATOM C CA ILE A 350 . −35.531 −2.326 4.650 1.00 21.78 . 1 2710 ATOM C C ILE A 350 . −36.397 −1.919 3.485 1.00 20.48 . 1 2711 ATOM O O ILE A 350 . −35.994 −1.128 2.674 1.00 21.13 . 1 2712 ATOM C CB ILE A 350 . −35.718 −1.369 5.865 1.00 21.11 . 1 2713 ATOM C CG1 ILE A 350 . −35.087 −0.029 5.589 1.00 21.66 . 1 2714 ATOM C CG2 ILE A 350 . −35.046 −1.968 7.120 1.00 22.29 . 1 2715 ATOM C CD1 ILE A 350 . −35.388 0.926 6.759 1.00 20.86 . 1 2716 ATOM N N TYR A 351 . −37.626 −2.446 3.436 1.00 20.51 . 1 2717 ATOM C CA TYR A 351 . −38.524 −2.229 2.289 1.00 21.67 . 1 2718 ATOM C C TYR A 351 . −39.816 −1.550 2.674 1.00 22.01 . 1 2719 ATOM O O TYR A 351 . −40.573 −2.049 3.518 1.00 24.27 . 1 2720 ATOM C CB TYR A 351 . −38.770 −3.613 1.637 1.00 21.94 . 1 2721 ATOM C CG TYR A 351 . −37.470 −4.302 1.286 1.00 23.40 . 1 2722 ATOM C CD1 TYR A 351 . −36.880 −5.179 2.180 1.00 23.09 . 1 2723 ATOM C CD2 TYR A 351 . −36.818 −4.040 0.087 1.00 24.63 . 1 2724 ATOM C CE1 TYR A 351 . −35.673 −5.794 1.888 1.00 25.89 . 1 2725 ATOM C CE2 TYR A 351 . −35.593 −4.637 −0.215 1.00 27.15 . 1 2726 ATOM C CZ TYR A 351 . −35.032 −5.527 0.721 1.00 27.10 . 1 2727 ATOM O OH TYR A 351 . −33.783 −6.114 0.531 1.00 31.97 . 1 2728 ATOM N N PRO A 352 . −40.089 −0.375 2.057 1.00 23.16 . 1 2729 ATOM C CA PRO A 352 . −41.298 0.371 2.373 1.00 25.30 . 1 2730 ATOM C C PRO A 352 . −42.629 −0.252 2.013 1.00 27.62 . 1 2731 ATOM O O PRO A 352 . −43.579 0.045 2.770 1.00 30.91 . 1 2732 ATOM C CB PRO A 352 . −41.054 1.733 1.703 1.00 24.82 . 1 2733 ATOM C CG PRO A 352 . −40.239 1.370 0.516 1.00 26.51 . 1 2734 ATOM C CD PRO A 352 . −39.247 0.338 1.071 1.00 24.22 . 1 2735 #352 . TER # . . PRO A 352 . . . . . . . 1 2736 HETA N N SAM . 1699 . −21.320 7.591 5.840 1.00 20.83 . 2 2737 HETA C CA SAM . 1699 . −20.040 8.342 6.321 1.00 24.01 . 2 2738 HETA C C SAM . 1699 . −18.931 7.281 6.519 1.00 22.98 . 2 2739 HETA O O SAM . 1699 . −17.728 7.712 6.654 1.00 22.85 . 2 2740 HETA O OXT SAM . 1699 . −19.285 6.059 6.585 1.00 22.86 . 2 2741 HETA C CB SAM . 1699 . −20.345 8.969 7.606 1.00 25.12 . 2 2742 HETA C CG SAM . 1699 . −19.522 9.785 8.514 1.00 29.71 . 2 2743 HETA S SD SAM . 1699 . −20.389 9.972 10.133 1.00 24.10 . 2 2744 HETA C CE SAM . 1699 . −20.444 8.358 10.760 1.00 31.40 . 2 2745 HETA C C5* SAM . 1699 . −22.041 10.684 9.519 1.00 28.08 . 2 2746 HETA C C4* SAM . 1699 . −22.149 11.542 9.363 1.00 24.09 . 2 2747 HETA O O4* SAM . 1699 . −23.583 11.953 9.223 1.00 20.60 . 2 2748 HETA C C3* SAM . 1699 . −21.303 12.823 9.096 1.00 20.72 . 2 2749 HETA O O3* SAM . 1699 . −20.714 12.881 7.724 1.00 20.22 . 2 2750 HETA C C2* SAM . 1699 . −22.266 13.931 9.398 1.00 20.77 . 2 2751 HETA O O2* SAM . 1699 . −21.937 15.179 8.783 1.00 20.41 . 2 2752 HETA C C1* SAM . 1699 . −23.682 13.427 9.150 1.00 21.86 . 2 2753 HETA N N9 SAM . 1699 . −24.835 14.186 9.370 1.00 20.30 . 2 2754 HETA C C8 SAM . 1699 . −25.109 14.543 10.674 1.00 20.02 . 2 2755 HETA N N7 SAM . 1699 . −26.197 15.202 10.769 1.00 20.30 . 2 2756 HETA C C5 SAM . 1699 . −26.658 15.281 9.463 1.00 19.55 . 2 2757 HETA C C6 SAM . 1699 . −27.852 15.903 8.901 1.00 20.67 . 2 2758 HETA N N6 SAM . 1699 . −28.708 16.522 9.679 1.00 21.93 . 2 2759 HETA N N1 SAM . 1699 . −27.976 15.768 7.540 1.00 21.49 . 2 2760 HETA C C2 SAM . 1699 . −27.091 15.122 6.739 1.00 21.73 . 2 2761 HETA N N3 SAM . 1699 . −25.961 14.538 7.228 1.00 20.40 . 2 2762 HETA C C4 SAM . 1699 . −25.827 14.656 8.569 1.00 21.71 . 2 2763 HETA O O HOH . 1 . 15.897 1.431 34.880 1.00 30.37 . 3 2764 HETA O O HOH . 2 . 1.282 10.335 24.860 1.00 22.41 . 3 2765 HETA O O HOH . 3 . −25.944 −0.498 15.533 1.00 23.83 . 3 2766 HETA O O HOH . 4 . −28.593 −2.808 22.228 1.00 27.61 . 3 2767 HETA O O HOH . 5 . −20.636 6.673 3.281 1.00 20.65 . 3 2768 HETA O O HOH . 6 . −18.151 7.932 2.741 1.00 22.25 . 3 2769 HETA O O HOH . 7 . −27.795 1.484 15.857 1.00 24.64 . 3 2770 HETA O O HOH . 8 . 11.640 7.988 36.159 1.00 26.43 . 3 2771 HETA O O HOH . 9 . −32.131 18.967 2.856 1.00 23.55 . 3 2772 HETA O O HOH . 10 . −20.739 14.940 36.038 1.00 25.16 . 3 2773 HETA O O HOH . 11 . −23.318 −9.474 19.573 1.00 27.95 . 3 2774 HETA O O HOH . 12 . −15.601 3.892 7.391 1.00 24.10 . 3 2775 HETA O O HOH . 13 . −25.480 12.228 −9.402 1.00 26.92 . 3 2776 HETA O O HOH . 14 . −24.051 7.102 4.876 1.00 22.13 . 3 2777 HETA O O HOH . 15 . 0.956 4.077 14.675 1.00 26.14 . 3 2778 HETA O O HOH . 16 . −43.759 −1.699 −1.900 1.00 28.97 . 3 2779 HETA O O HOH . 17 . −26.437 6.584 24.401 1.00 25.63 . 3 2780 HETA O O HOH . 18 . −25.129 10.901 11.639 1.00 24.96 . 3 2781 HETA O O HOH . 19 . −5.149 11.745 20.808 1.00 27.59 . 3 2782 HETA O O HOH . 20 . −30.006 6.150 22.654 1.00 28.61 . 3 2783 HETA O O HOH . 21 . −20.131 8.689 0.000 1.00 22.46 . 3 2784 HETA O O HOH . 22 . −35.799 −11.872 −2.193 1.00 22.98 . 3 2785 HETA O O HOH . 23 . −20.057 −5.804 28.582 1.00 30.40 . 3 2786 HETA O O HOH . 24 . −13.072 1.088 −6.094 1.00 29.75 . 3 2787 HETA O O HOH . 25 . −22.383 0.506 14.144 1.00 24.71 . 3 2788 HETA O O HOH . 26 . 4.317 −5.203 32.072 1.00 29.17 . 3 2789 HETA O O HOH . 27 . −23.044 −6.701 13.108 1.00 23.52 . 3 2790 HETA O O HOH . 28 . −30.930 18.069 28.374 1.00 29.48 . 3 2791 HETA O O HOH . 29 . −27.485 17.346 34.479 1.00 29.18 . 3 2792 HETA O O HOH . 30 . −26.505 3.726 9.564 1.00 20.56 . 3 2793 HETA O O HOH . 31 . −18.486 13.904 37.096 1.00 27.48 . 3 2794 HETA O O HOH . 32 . −16.520 5.602 3.568 1.00 23.96 . 3 2795 HETA O O HOH . 33 . −27.271 17.284 12.451 1.00 24.84 . 3 2796 HETA O O HOH . 34 . 10.737 −2.551 6.425 1.00 29.44 . 3 2797 HETA O O HOH . 35 . 13.681 5.731 33.429 1.00 26.49 . 3 2798 HETA O O HOH . 36 . 5.864 −2.954 32.558 1.00 28.30 . 3 2799 HETA O O HOH . 37 . 7.272 4.395 32.753 1.00 27.78 . 3 2800 HETA O O HOH . 38 . −32.690 5.944 22.019 1.00 24.75 . 3 2801 HETA O O HOH . 39 . −40.408 −2.466 −5.207 1.00 31.01 . 3 2802 HETA O O HOH . 40 . −30.715 19.367 11.984 1.00 37.57 . 3 2803 HETA O O HOH . 41 . −21.618 18.026 −7.535 1.00 33.42 . 3 2804 HETA O O HOH . 42 . −16.627 10.199 3.485 1.00 24.40 . 3 2805 HETA O O HOH . 43 . −13.826 10.135 22.219 1.00 29.07 . 3 2806 HETA O O HOH . 44 . −23.990 −1.943 25.960 1.00 27.41 . 3 2807 HETA O O HOH . 45 . −27.588 12.373 18.409 1.00 25.89 . 3 2808 HETA O O HOH . 46 . −14.266 −1.885 10.872 1.00 30.76 . 3 2809 HETA O O HOH . 47 . −30.083 −9.686 17.524 1.00 27.14 . 3 2810 HETA O O HOH . 48 . −23.076 22.787 7.528 1.00 31.72 . 3 2811 HETA O O HOH . 49 . −15.205 6.968 5.585 1.00 29.68 . 3 2812 HETA O O HOH . 50 . −32.560 13.458 22.809 1.00 31.14 . 3 2813 HETA O O HOH . 51 . −39.703 10.584 16.157 1.00 30.21 . 3 2814 HETA O O HOH . 52 . −7.683 10.987 13.385 1.00 30.68 . 3 2815 HETA O O HOH . 53 . −15.695 8.126 22.212 1.00 27.90 . 3 2816 HETA O O HOH . 54 . 6.475 6.778 9.398 1.00 37.29 . 3 2817 HETA O O HOH . 55 . −26.951 17.560 22.569 1.00 33.64 . 3 2818 HETA O O HOH . 56 . −30.161 11.557 19.079 1.00 25.08 . 3 2819 HETA O O HOH . 57 . 12.836 3.597 34.999 1.00 27.56 . 3 2820 HETA O O HOH . 58 . −30.088 13.178 21.488 1.00 28.36 . 3 2821 HETA O O HOH . 59 . −17.588 9.039 34.801 1.00 21.81 . 3 2822 HETA O O HOH . 60 . −24.312 16.065 19.999 1.00 27.65 . 3 2823 HETA O O HOH . 61 . −31.787 10.383 −7.926 1.00 35.29 . 3 2824 HETA O O HOH . 62 . −39.051 13.037 9.745 1.00 29.25 . 3 2825 HETA O O HOH . 63 . −1.372 −10.179 20.103 1.00 34.22 . 3 2826 HETA O O HOH . 64 . 8.964 9.313 16.806 1.00 34.41 . 3 2827 HETA O O HOH . 65 . −39.716 −1.849 −1.689 1.00 32.34 . 3 2828 HETA O O HOH . 66 . −29.408 −7.811 3.899 1.00 28.57 . 3 2829 HETA O O HOH . 67 . 14.001 9.429 35.741 1.00 28.27 . 3 2830 HETA O O HOH . 68 . −12.972 6.250 −2.122 1.00 31.03 . 3 2831 HETA O O HOH . 69 . −19.620 16.235 10.096 1.00 35.69 . 3 2832 HETA O O HOH . 70 . −17.898 12.652 7.457 1.00 34.51 . 3 2833 HETA O O HOH . 71 . −7.346 7.564 7.754 1.00 34.86 . 3 2834 HETA O O HOH . 72 . −6.241 −2.636 33.800 1.00 32.65 . 3 2835 HETA O O HOH . 73 . −37.806 −9.894 4.981 1.00 27.41 . 3 2836 HETA O O HOH . 74 . 2.511 9.534 15.450 1.00 39.29 . 3 2837 HETA O O HOH . 75 . −32.739 −11.107 8.430 1.00 28.61 . 3 2838 HETA O O HOH . 76 . −28.696 −9.965 21.342 1.00 36.41 . 3 2839 HETA O O HOH . 77 . −5.807 4.982 8.036 1.00 30.49 . 3 2840 HETA O O HOH . 78 . 21.113 −3.074 19.341 1.00 34.67 . 3 2841 HETA O O HOH . 79 . −35.564 16.914 14.277 1.00 36.45 . 3 2842 HETA O O HOH . 80 . 17.551 −3.568 16.779 1.00 27.47 . 3 2843 HETA O O HOH . 81 . −9.572 23.096 15.583 1.00 38.13 . 3 2844 HETA O O HOH . 82 . 16.401 5.527 32.669 1.00 28.90 . 3 2845 HETA O O HOH . 83 . 3.752 4.218 14.393 1.00 26.96 . 3 2846 HETA O O HOH . 84 . 5.833 −7.909 29.129 1.00 30.84 . 3 2847 HETA O O HOH . 85 . −21.379 5.881 −11.685 1.00 29.22 . 3 2848 HETA O O HOH . 86 . −2.776 −1.000 25.871 1.00 32.17 . 3 2849 HETA O O HOH . 87 . −28.495 5.266 −13.943 1.00 33.98 . 3 2850 HETA O O HOH . 88 . 8.258 −6.969 13.749 1.00 35.22 . 3 2851 HETA O O HOH . 89 . −18.400 −13.590 15.966 1.00 42.01 . 3 2852 HETA O O HOH . 90 . 0.569 4.914 11.254 1.00 27.71 . 3 2853 HETA O O HOH . 91 . −19.284 −8.538 0.472 1.00 28.61 . 3 2854 HETA O O HOH . 92 . −2.262 0.022 47.323 1.00 35.63 . 3 2855 HETA O O HOH . 93 . −28.232 −0.757 23.987 1.00 31.39 . 3 2856 HETA O O HOH . 94 . −0.076 −5.336 30.375 1.00 30.10 . 3 2857 HETA O O HOH . 95 . −8.968 11.395 31.383 1.00 39.26 . 3 2858 HETA O O HOH . 96 . −2.847 11.969 19.258 1.00 27.83 . 3 2859 HETA O O HOH . 97 . −6.027 −6.809 50.501 1.00 35.95 . 3 2860 HETA O O HOH . 98 . 13.121 2.420 11.935 1.00 26.71 . 3 2861 HETA O O HOH . 99 . −13.782 −5.920 2.094 1.00 32.49 . 3 2862 HETA O O HOH . 100 . −17.151 16.153 8.827 1.00 37.56 . 3 2863 HETA O O HOH . 101 . −8.667 14.465 29.338 1.00 33.92 . 3 2864 HETA O O HOH . 102 . −33.074 13.574 −6.489 1.00 29.12 . 3 2865 HETA O O HOH . 103 . −38.539 8.159 −4.928 1.00 28.98 . 3 2866 HETA O O HOH . 104 . −17.407 20.114 9.198 1.00 44.71 . 3 2867 HETA O O HOH . 105 . −40.568 7.226 10.999 1.00 35.30 . 3 2868 HETA O O HOH . 106 . −15.118 −7.150 −7.092 1.00 39.53 . 3 2869 HETA O O HOH . 107 . −14.294 23.035 10.435 1.00 34.08 . 3 2870 HETA O O HOH . 108 . −34.328 11.919 21.160 1.00 29.46 . 3 2871 HETA O O HOH . 109 . −13.689 17.302 28.076 1.00 36.74 . 3 2872 HETA O O HOH . 110 . −39.235 −8.509 8.209 1.00 32.80 . 3 2873 HETA O O HOH . 111 . −35.752 7.825 21.797 1.00 34.69 . 3 2874 HETA O O HOH . 112 . −14.559 −7.287 −0.226 1.00 34.68 . 3 2875 HETA O O HOH . 113 . −22.222 −13.802 22.234 1.00 31.10 . 3 2876 HETA O O HOH . 114 . 0.823 11.557 16.531 1.00 37.01 . 3 2877 HETA O O HOH . 115 . −16.493 9.440 −15.359 1.00 39.80 . 3 2878 HETA O O HOH . 116 . −22.422 −9.795 28.339 1.00 36.87 . 3 2879 HETA O O HOH . 117 . −37.363 2.717 −7.122 1.00 33.79 . 3 2880 HETA O O HOH . 118 . −19.849 1.018 15.067 1.00 31.66 . 3 2881 HETA O O HOH . 119 . −42.282 8.979 5.247 1.00 33.31 . 3 2882 HETA O O HOH . 120 . −20.131 −6.319 −7.372 1.00 33.40 . 3 2883 HETA O O HOH . 121 . −30.886 −0.286 24.279 1.00 31.31 . 3 2884 HETA O O HOH . 122 . −27.609 −11.621 1.846 1.00 39.83 . 3 2885 HETA O O HOH . 123 . 20.563 3.928 23.067 1.00 40.11 . 3 2886 HETA O O HOH . 124 . −6.214 17.096 13.366 1.00 39.26 . 3 2887 HETA O O HOH . 125 . −24.528 −9.993 14.338 1.00 36.53 . 3 2888 HETA O O HOH . 126 . −6.821 1.907 6.470 1.00 32.43 . 3 2889 HETA O O HOH . 127 . −17.153 5.616 −12.598 1.00 37.20 . 3 2890 HETA O O HOH . 128 . −9.871 −0.087 5.369 1.00 34.69 . 3 2891 HETA O O HOH . 129 . 0.612 −11.629 16.229 1.00 37.00 . 3 2892 HETA O O HOH . 130 . 16.273 −5.243 8.813 1.00 36.84 . 3 2893 HETA O O HOH . 131 . −17.933 −4.769 26.900 1.00 36.44 . 3 2894 HETA O O HOH . 132 . −17.534 9.170 −10.825 1.00 38.41 . 3 2895 HETA O O HOH . 133 . 18.953 12.223 31.252 1.00 36.61 . 3 2896 HETA O O HOH . 134 . −28.746 −7.549 23.220 1.00 38.52 . 3 2897 HETA O O HOH . 135 . −27.630 20.306 7.682 1.00 26.55 . 3 2898 HETA O O HOH . 136 . −2.566 −6.476 10.920 1.00 40.74 . 3 2899 HETA O O HOH . 137 . −8.270 −3.535 28.180 1.00 34.97 . 3 2900 HETA O O HOH . 138 . −33.843 4.211 24.018 1.00 37.77 . 3 2901 HETA O O HOH . 139 . −5.262 −10.416 44.514 1.00 35.23 . 3 2902 HETA O O HOH . 140 . −27.335 16.023 −7.873 1.00 35.92 . 3 2903 HETA O O HOH . 141 . −12.099 −8.923 59.087 1.00 41.18 . 3 2904 HETA O O HOH . 142 . −32.832 18.002 31.882 1.00 33.16 . 3 2905 HETA O O HOH . 143 . −1.996 7.861 13.306 1.00 35.07 . 3 2906

APPENDIX C ATOM TYPE RES # X Y Z OCC B ATOM ATOM N N GLN D 19 . 32.835 9.393 55.840 1.00 53.11 . 1 1 ATOM C CA GLN D 19 . 33.308 8.312 56.695 1.00 51.93 . 1 2 ATOM C C GLN D 19 . 34.692 7.998 56.573 1.00 49.16 . 1 3 ATOM O O GLN D 19 . 35.257 8.091 55.456 1.00 50.05 . 1 4 ATOM C CB GLN D 19 . 32.440 7.065 56.515 1.00 52.33 . 1 5 ATOM C CG GLN D 19 . 32.601 6.375 55.161 1.00 52.88 . 1 6 ATOM C CD GLN D 19 . 31.555 5.275 54.945 1.00 51.28 . 1 7 ATOM O OE1 GLN D 19 . 30.889 4.865 55.896 1.00 53.66 . 1 8 ATOM N NE2 GLN D 19 . 31.356 4.766 53.745 1.00 52.46 . 1 9 ATOM N N THR D 20 . 34.940 7.699 57.782 1.00 47.49 . 1 10 ATOM C CA THR D 20 . 36.128 7.257 58.288 1.00 43.22 . 1 11 ATOM C C THR D 20 . 36.217 5.834 58.064 1.00 41.12 . 1 12 ATOM O O THR D 20 . 35.207 5.101 58.138 1.00 39.37 . 1 13 ATOM C CB THR D 20 . 36.182 7.452 59.795 1.00 44.35 . 1 14 ATOM O OG1 THR D 20 . 35.102 6.767 60.418 1.00 44.89 . 1 15 ATOM C CG2 THR D 20 . 36.102 8.916 60.200 1.00 46.48 . 1 16 ATOM N N GLU D 21 . 37.390 5.605 57.806 1.00 38.95 . 1 17 ATOM C CA GLU D 21 . 37.849 4.354 57.665 1.00 35.02 . 1 18 ATOM C C GLU D 21 . 37.402 3.587 58.897 1.00 32.46 . 1 19 ATOM O O GLU D 21 . 36.955 2.450 58.805 1.00 28.92 . 1 20 ATOM C CB GLU D 21 . 39.373 4.463 57.639 1.00 36.23 . 1 21 ATOM C CG GLU D 21 . 40.058 3.297 56.969 1.00 36.76 . 1 22 ATOM C CD GLU D 21 . 39.434 2.940 55.629 1.00 37.97 . 1 23 ATOM O OE1 GLU D 21 . 38.518 2.037 55.574 1.00 34.96 . 1 24 ATOM O OE2 GLU D 21 . 39.824 3.539 54.558 1.00 38.25 . 1 25 ATOM N N ASP D 22 . 37.529 4.219 60.069 1.00 30.48 . 1 26 ATOM C CA ASP D 22 . 37.139 3.557 61.339 1.00 29.85 . 1 27 ATOM C C ASP D 22 . 35.645 3.228 61.283 1.00 30.15 . 1 28 ATOM O O ASP D 22 . 35.220 2.145 61.685 1.00 27.53 . 1 29 ATOM C CB ASP D 22 . 37.435 4.452 62.535 1.00 31.50 . 1 30 ATOM C CG ASP D 22 . 38.889 4.352 62.987 1.00 32.93 . 1 31 ATOM O OD1 ASP D 22 . 39.434 3.198 63.169 1.00 33.81 . 1 32 ATOM O OD2 ASP D 22 . 39.570 5.428 63.175 1.00 35.34 . 1 33 ATOM N N SER D 23 . 34.849 4.165 60.774 1.00 27.44 . 1 34 ATOM C CA SER D 23 . 33.409 3.951 60.665 1.00 28.80 . 1 35 ATOM C C SER D 23 . 33.064 2.898 59.619 1.00 25.91 . 1 36 ATOM O O SER D 23 . 32.184 2.065 59.835 1.00 28.21 . 1 37 ATOM C CB SER D 23 . 32.694 5.259 60.322 1.00 29.66 . 1 38 ATOM O OG SER D 23 . 32.724 6.136 61.429 1.00 37.67 . 1 39 ATOM N N ALA D 24 . 33.757 2.939 58.490 1.00 26.25 . 1 40 ATOM C CA ALA D 24 . 33.512 1.982 57.417 1.00 25.99 . 1 41 ATOM C C ALA D 24 . 33.808 0.562 57.870 1.00 27.17 . 1 42 ATOM O O ALA D 24 . 33.039 −0.358 57.594 1.00 27.70 . 1 43 ATOM C CB ALA D 24 . 34.358 2.321 56.199 1.00 24.34 . 1 44 ATOM N N CYS D 25 . 34.930 0.373 58.552 1.00 25.83 . 1 45 ATOM C CA CYS D 25 . 35.273 −0.960 59.008 1.00 26.81 . 1 46 ATOM C C CYS D 25 . 34.286 −1.421 60.074 1.00 26.70 . 1 47 ATOM O O CYS D 25 . 33.869 −2.577 60.071 1.00 27.26 . 1 48 ATOM C CB CYS D 25 . 36.699 −0.996 59.548 1.00 26.10 . 1 49 ATOM S SG CYS D 25 . 37.303 −2.681 59.824 1.00 30.04 . 1 50 ATOM N N LEU D 26 . 33.900 −0.525 60.983 1.00 26.48 . 1 51 ATOM C CA LEU D 26 . 32.933 −0.895 62.008 1.00 25.98 . 1 52 ATOM C C LEU D 26 . 31.654 −1.401 61.340 1.00 26.50 . 1 53 ATOM O O LEU D 26 . 31.093 −2.421 61.750 1.00 23.65 . 1 54 ATOM C CB LEU D 26 . 32.605 0.298 62.923 1.00 26.30 . 1 55 ATOM C CG LEU D 26 . 31.422 0.131 63.886 1.00 26.34 . 1 56 ATOM C CD1 LEU D 26 . 31.640 −1.075 64.799 1.00 26.86 . 1 57 ATOM C CD2 LEU D 26 . 31.258 1.410 64.718 1.00 27.11 . 1 58 ATOM N N SER D 27 . 31.188 −0.691 60.312 1.00 25.34 . 1 59 ATOM C CA SER D 27 . 29.976 −1.112 59.608 1.00 26.01 . 1 60 ATOM C C SER D 27 . 30.166 −2.470 58.949 1.00 23.82 . 1 61 ATOM O O SER D 27 . 29.257 −3.298 58.950 1.00 25.10 . 1 62 ATOM C CB SER D 27 . 29.583 −0.087 58.534 1.00 27.77 . 1 63 ATOM O OG SER D 27 . 28.978 1.040 59.144 1.00 33.53 . 1 64 ATOM N N ALA D 28 . 31.341 −2.692 58.376 1.00 23.96 . 1 65 ATOM C CA ALA D 28 . 31.615 −3.965 57.720 1.00 25.47 . 1 66 ATOM C C ALA D 28 . 31.592 −5.103 58.743 1.00 25.76 . 1 67 ATOM O O ALA D 28 . 31.194 −6.225 58.430 1.00 24.35 . 1 68 ATOM C CB ALA D 28 . 32.958 −3.920 57.019 1.00 24.13 . 1 69 ATOM N N MET D 29 . 32.017 −4.815 59.969 1.00 24.05 . 1 70 ATOM C CA MET D 29 . 32.017 −5.843 61.005 1.00 23.43 . 1 71 ATOM C C MET D 29 . 30.587 −6.148 61.433 1.00 24.15 . 1 72 ATOM O O MET D 29 . 30.234 −7.303 61.667 1.00 26.62 . 1 73 ATOM C CB MET D 29 . 32.857 −5.398 62.205 1.00 23.71 . 1 74 ATOM C CG MET D 29 . 34.346 −5.262 61.896 1.00 23.60 . 1 75 ATOM S SD MET D 29 . 35.259 −4.742 63.380 1.00 25.05 . 1 76 ATOM C CE MET D 29 . 36.843 −5.283 62.985 1.00 23.75 . 1 77 ATOM N N VAL D 30 . 29.757 −5.115 61.531 1.00 22.65 . 1 78 ATOM C CA VAL D 30 . 28.368 −5.304 61.903 1.00 23.11 . 1 79 ATOM C C VAL D 30 . 27.675 −6.099 60.797 1.00 25.46 . 1 80 ATOM O O VAL D 30 . 26.903 −7.025 61.066 1.00 25.20 . 1 81 ATOM C CB VAL D 30 . 27.639 −3.944 62.055 1.00 25.80 . 1 82 ATOM C CG1 VAL D 30 . 26.144 −4.154 62.254 1.00 24.42 . 1 83 ATOM C CG2 VAL D 30 . 28.217 −3.183 63.239 1.00 25.54 . 1 84 ATOM N N LEU D 31 . 27.972 −5.733 59.555 1.00 24.61 . 1 85 ATOM C CA LEU D 31 . 27.354 −6.370 58.400 1.00 25.57 . 1 86 ATOM C C LEU D 31 . 27.857 −7.763 58.036 1.00 25.66 . 1 87 ATOM O O LEU D 31 . 27.320 −8.397 57.130 1.00 26.77 . 1 88 ATOM C CB LEU D 31 . 27.459 −5.434 57.190 1.00 26.37 . 1 89 ATOM C CG LEU D 31 . 26.570 −4.197 57.357 1.00 30.46 . 1 90 ATOM C CD1 LEU D 31 . 26.884 −3.151 56.299 1.00 31.68 . 1 91 ATOM C CD2 LEU D 31 . 25.117 −4.622 57.280 1.00 30.93 . 1 92 ATOM N N THR D 32 . 28.878 −8.250 58.730 1.00 24.76 . 1 93 ATOM C CA THR D 32 . 29.378 −9.590 58.451 1.00 24.87 . 1 94 ATOM C C THR D 32 . 29.115 −10.527 59.620 1.00 25.12 . 1 95 ATOM O O THR D 32 . 29.332 −11.732 59.517 1.00 26.44 . 1 96 ATOM C CB THR D 32 . 30.893 −9.597 58.142 1.00 24.44 . 1 97 ATOM O OG1 THR D 32 . 31.592 −8.818 59.120 1.00 25.83 . 1 98 ATOM C CG2 THR D 32 . 31.157 −9.035 56.757 1.00 25.18 . 1 99 ATOM N N THR D 33 . 28.636 −9.978 60.731 1.00 24.37 . 1 100 ATOM C CA THR D 33 . 28.375 −10.795 61.907 1.00 25.23 . 1 101 ATOM C C THR D 33 . 26.931 −10.727 62.367 1.00 26.59 . 1 102 ATOM O O THR D 33 . 26.579 −11.341 63.379 1.00 26.46 . 1 103 ATOM C CB THR D 33 . 29.262 −10.353 63.098 1.00 26.44 . 1 104 ATOM O OG1 THR D 33 . 28.882 −9.035 63.502 1.00 26.66 . 1 105 ATOM C CG2 THR D 33 . 30.722 −10.335 62.708 1.00 23.55 . 1 106 ATOM N N ASN D 34 . 26.080 −10.013 61.629 1.00 26.63 . 1 107 ATOM C CA ASN D 34 . 24.699 −9.867 62.067 1.00 27.81 . 1 108 ATOM C C ASN D 34 . 23.769 −11.075 62.001 1.00 28.21 . 1 109 ATOM O O ASN D 34 . 22.559 −10.942 62.187 1.00 25.83 . 1 110 ATOM C CB ASN D 34 . 24.027 −8.634 61.419 1.00 27.53 . 1 111 ATOM C CG ASN D 34 . 23.891 −8.735 59.909 1.00 29.88 . 1 112 ATOM O OD1 ASN D 34 . 24.196 −9.756 59.296 1.00 27.23 . 1 113 ATOM N ND2 ASN D 34 . 23.408 −7.651 59.302 1.00 26.27 . 1 114 ATOM N N LEU D 35 . 24.326 −12.257 61.759 1.00 27.42 . 1 115 ATOM C CA LEU D 35 . 23.503 −13.455 61.771 1.00 26.38 . 1 116 ATOM C C LEU D 35 . 23.087 −13.643 63.240 1.00 26.35 . 1 117 ATOM O O LEU D 35 . 22.064 −14.255 63.552 1.00 21.93 . 1 118 ATOM C CB LEU D 35 . 24.320 −14.662 61.290 1.00 28.72 . 1 119 ATOM C CG LEU D 35 . 23.637 −16.027 61.416 1.00 30.75 . 1 120 ATOM C CD1 LEU D 35 . 22.358 −16.039 60.588 1.00 30.18 . 1 121 ATOM C CD2 LEU D 35 . 24.593 −17.129 60.956 1.00 31.44 . 1 122 ATOM N N VAL D 36 . 23.879 −13.082 64.151 1.00 25.44 . 1 123 ATOM C CA VAL D 36 . 23.585 −13.213 65.577 1.00 25.70 . 1 124 ATOM C C VAL D 36 . 22.274 −12.558 65.988 1.00 25.46 . 1 125 ATOM O O VAL D 36 . 21.548 −13.093 66.826 1.00 25.26 . 1 126 ATOM C CB VAL D 36 . 24.726 −12.624 66.446 1.00 24.71 . 1 127 ATOM C CG1 VAL D 36 . 24.373 −12.729 67.917 1.00 25.11 . 1 128 ATOM C CG2 VAL D 36 . 26.005 −13.360 66.176 1.00 25.98 . 1 129 ATOM N N TYR D 37 . 21.952 −11.410 65.399 1.00 24.31 . 1 130 ATOM C CA TYR D 37 . 20.724 −10.715 65.770 1.00 24.20 . 1 131 ATOM C C TYR D 37 . 19.469 −11.585 65.612 1.00 24.22 . 1 132 ATOM O O TYR D 37 . 18.687 −11.733 66.550 1.00 24.57 . 1 133 ATOM C CB TYR D 37 . 20.584 −9.406 64.973 1.00 24.67 . 1 134 ATOM C CG TYR D 37 . 19.221 −8.791 65.119 1.00 25.43 . 1 135 ATOM C CD1 TYR D 37 . 18.798 −8.264 66.344 1.00 24.75 . 1 136 ATOM C CD2 TYR D 37 . 18.309 −8.830 64.066 1.00 26.14 . 1 137 ATOM C CE1 TYR D 37 . 17.499 −7.802 66.511 1.00 27.27 . 1 138 ATOM C CE2 TYR D 37 . 17.013 −8.372 64.227 1.00 25.60 . 1 139 ATOM C CZ TYR D 37 . 16.614 −7.863 65.450 1.00 26.08 . 1 140 ATOM O OH TYR D 37 . 15.319 −7.445 65.612 1.00 27.63 . 1 141 ATOM N N PRO D 38 . 19.256 −12.172 64.423 1.00 25.29 . 1 142 ATOM C CA PRO D 38 . 18.070 −13.014 64.247 1.00 25.25 . 1 143 ATOM C C PRO D 38 . 18.079 −14.201 65.221 1.00 26.68 . 1 144 ATOM O O PRO D 38 . 17.030 −14.668 65.656 1.00 25.10 . 1 145 ATOM C CB PRO D 38 . 18.182 −13.469 62.799 1.00 26.45 . 1 146 ATOM C CG PRO D 38 . 18.896 −12.347 62.144 1.00 28.85 . 1 147 ATOM C CD PRO D 38 . 19.968 −12.002 63.147 1.00 28.08 . 1 148 ATOM N N ALA D 39 . 19.271 −14.690 65.550 1.00 28.56 . 1 149 ATOM C CA ALA D 39 . 19.399 −15.812 66.482 1.00 29.14 . 1 150 ATOM C C ALA D 39 . 18.910 −15.378 67.860 1.00 28.22 . 1 151 ATOM O O ALA D 39 . 18.149 −16.090 68.521 1.00 27.92 . 1 152 ATOM C CB ALA D 39 . 20.851 −16.253 66.561 1.00 29.48 . 1 153 ATOM N N VAL D 40 . 19.358 −14.204 68.296 1.00 26.58 . 1 154 ATOM C CA VAL D 40 . 18.953 −13.674 69.587 1.00 25.36 . 1 155 ATOM C C VAL D 40 . 17.463 −13.336 69.582 1.00 25.91 . 1 156 ATOM O O VAL D 40 . 16.740 −13.666 70.524 1.00 26.01 . 1 157 ATOM C CB VAL D 40 . 19.785 −12.425 69.944 1.00 26.23 . 1 158 ATOM C CG1 VAL D 40 . 19.215 −11.737 71.173 1.00 25.17 . 1 159 ATOM C CG2 VAL D 40 . 21.224 −12.830 70.175 1.00 26.69 . 1 160 ATOM N N LEU D 41 . 16.990 −12.696 68.517 1.00 27.32 . 1 161 ATOM C CA LEU D 41 . 15.573 −12.351 68.432 1.00 25.37 . 1 162 ATOM C C LEU D 41 . 14.702 −13.602 68.526 1.00 25.91 . 1 163 ATOM O O LEU D 41 . 13.712 −13.621 69.251 1.00 26.21 . 1 164 ATOM C CB LEU D 41 . 15.271 −11.613 67.121 1.00 26.66 . 1 165 ATOM C CG LEU D 41 . 13.793 −11.366 66.791 1.00 24.29 . 1 166 ATOM C CD1 LEU D 41 . 13.167 −10.487 67.850 1.00 24.62 . 1 167 ATOM C CD2 LEU D 41 . 13.672 −10.692 65.421 1.00 26.43 . 1 168 ATOM N N ASN D 42 . 15.081 −14.637 67.782 1.00 28.43 . 1 169 ATOM C CA ASN D 42 . 14.354 −15.906 67.748 1.00 29.56 . 1 170 ATOM C C ASN D 42 . 14.234 −16.492 69.157 1.00 30.31 . 1 171 ATOM O O ASN D 42 . 13.184 −17.010 69.545 1.00 28.12 . 1 172 ATOM C CB ASN D 42 . 15.098 −16.884 66.834 1.00 31.57 . 1 173 ATOM C CG ASN D 42 . 14.384 −18.217 66.681 1.00 34.92 . 1 174 ATOM O OD1 ASN D 42 . 14.991 −19.272 66.863 1.00 36.48 . 1 175 ATOM N ND2 ASN D 42 . 13.099 −18.177 66.326 1.00 32.96 . 1 176 ATOM N N ALA D 43 . 15.322 −16.405 69.913 1.00 29.79 . 1 177 ATOM C CA ALA D 43 . 15.346 −16.907 71.283 1.00 31.28 . 1 178 ATOM C C ALA D 43 . 14.436 −16.059 72.182 1.00 31.77 . 1 179 ATOM O O ALA D 43 . 13.689 −16.591 73.009 1.00 30.66 . 1 180 ATOM C CB ALA D 43 . 16.778 −16.896 71.812 1.00 29.18 . 1 181 ATOM N N ALA D 44 . 14.491 −14.741 72.009 1.00 29.74 . 1 182 ATOM C CA ALA D 44 . 13.667 −13.835 72.797 1.00 29.41 . 1 183 ATOM C C ALA D 44 . 12.181 −14.108 72.567 1.00 29.00 . 1 184 ATOM O O ALA D 44 . 11.376 −14.061 73.496 1.00 27.78 . 1 185 ATOM C CB ALA D 44 . 13.998 −12.382 72.444 1.00 28.03 . 1 186 ATOM N N ILE D 45 . 11.821 −14.398 71.324 1.00 28.59 . 1 187 ATOM C CA ILE D 45 . 10.434 −14.673 70.987 1.00 27.86 . 1 188 ATOM C C ILE D 45 . 9.960 −15.967 71.666 1.00 29.86 . 1 189 ATOM O O ILE D 45 . 8.897 −15.995 72.281 1.00 29.02 . 1 190 ATOM C CB ILE D 45 . 10.264 −14.793 69.460 1.00 28.88 . 1 191 ATOM C CG1 ILE D 45 . 10.514 −13.426 68.804 1.00 27.52 . 1 192 ATOM C CG2 ILE D 45 . 8.872 −15.302 69.126 1.00 28.51 . 1 193 ATOM C CD1 ILE D 45 . 10.800 −13.487 67.312 1.00 27.72 . 1 194 ATOM N N ASP D 46 . 10.755 −17.027 71.553 1.00 31.36 . 1 195 ATOM C CA ASP D 46 . 10.407 −18.314 72.151 1.00 35.08 . 1 196 ATOM C C ASP D 46 . 10.377 −18.250 73.683 1.00 35.87 . 1 197 ATOM O O ASP D 46 . 9.706 −19.062 74.325 1.00 37.46 . 1 198 ATOM C CB ASP D 46 . 11.391 −19.401 71.697 1.00 36.19 . 1 199 ATOM C CG ASP D 46 . 11.220 −19.783 70.231 1.00 38.77 . 1 200 ATOM O OD1 ASP D 46 . 10.243 −19.334 69.588 1.00 37.32 . 1 201 ATOM O OD2 ASP D 46 . 12.067 −20.549 69.722 1.00 41.29 . 1 202 ATOM N N LEU D 47 . 11.100 −17.291 74.259 1.00 36.43 . 1 203 ATOM C CA LEU D 47 . 11.141 −17.110 75.711 1.00 36.57 . 1 204 ATOM C C LEU D 47 . 10.086 −16.096 76.142 1.00 36.74 . 1 205 ATOM O O LEU D 47 . 10.005 −15.730 77.317 1.00 37.09 . 1 206 ATOM C CB LEU D 47 . 12.529 −16.637 76.166 1.00 35.22 . 1 207 ATOM C CG LEU D 47 . 13.661 −17.668 76.122 1.00 36.25 . 1 208 ATOM C CD1 LEU D 47 . 14.974 −17.016 76.510 1.00 35.65 . 1 209 ATOM C CD2 LEU D 47 . 13.343 −18.821 77.070 1.00 35.79 . 1 210 ATOM N N ASN D 48 . 9.289 −15.649 75.171 1.00 36.52 . 1 211 ATOM C CA ASN D 48 . 8.201 −14.696 75.390 1.00 35.64 . 1 212 ATOM C C ASN D 48 . 8.623 −13.425 76.108 1.00 32.89 . 1 213 ATOM O O ASN D 48 . 7.839 −12.855 76.864 1.00 33.93 . 1 214 ATOM C CB ASN D 48 . 7.069 −15.357 76.192 1.00 39.00 . 1 215 ATOM C CG ASN D 48 . 6.784 −16.776 75.742 1.00 44.30 . 1 216 ATOM O OD1 ASN D 48 . 7.504 −17.717 76.099 1.00 48.21 . 1 217 ATOM N ND2 ASN D 48 . 5.733 −16.942 74.949 1.00 45.81 . 1 218 ATOM N N LEU D 49 . 9.848 −12.973 75.869 1.00 31.56 . 1 219 ATOM C CA LEU D 49 . 10.352 −11.771 76.531 1.00 30.56 . 1 220 ATOM C C LEU D 49 . 9.567 −10.505 76.217 1.00 30.88 . 1 221 ATOM O O LEU D 49 . 9.388 −9.645 77.084 1.00 30.15 . 1 222 ATOM C CB LEU D 49 . 11.823 −11.553 76.174 1.00 30.34 . 1 223 ATOM C CG LEU D 49 . 12.748 −12.729 76.488 1.00 29.62 . 1 224 ATOM C CD1 LEU D 49 . 14.182 −12.330 76.213 1.00 30.10 . 1 225 ATOM C CD2 LEU D 49 . 12.571 −13.135 77.949 1.00 31.30 . 1 226 ATOM N N PHE D 50 . 9.102 −10.381 74.977 1.00 30.29 . 1 227 ATOM C CA PHE D 50 . 8.355 −9.195 74.592 1.00 29.62 . 1 228 ATOM C C PHE D 50 . 6.985 −9.178 75.257 1.00 30.52 . 1 229 ATOM O O PHE D 50 . 6.525 −8.135 75.723 1.00 28.83 . 1 230 ATOM C CB PHE D 50 . 8.239 −9.122 73.063 1.00 27.55 . 1 231 ATOM C CG PHE D 50 . 9.562 −9.180 72.367 1.00 26.01 . 1 232 ATOM C CD1 PHE D 50 . 9.973 −10.339 71.719 1.00 23.24 . 1 233 ATOM C CD2 PHE D 50 . 10.432 −8.090 72.410 1.00 25.33 . 1 234 ATOM C CE1 PHE D 50 . 11.230 −10.414 71.128 1.00 24.88 . 1 235 ATOM C CE2 PHE D 50 . 11.685 −8.155 71.826 1.00 23.45 . 1 236 ATOM C CZ PHE D 50 . 12.091 −9.322 71.180 1.00 26.69 . 1 237 ATOM N N GLU D 51 . 6.332 −10.334 75.310 1.00 32.23 . 1 238 ATOM C CA GLU D 51 . 5.028 −10.410 75.950 1.00 34.25 . 1 239 ATOM C C GLU D 51 . 5.220 −10.054 77.426 1.00 35.25 . 1 240 ATOM O O GLU D 51 . 4.452 −9.279 78.002 1.00 34.27 . 1 241 ATOM C CB GLU D 51 . 4.454 −11.823 75.818 1.00 37.15 . 1 242 ATOM C CG GLU D 51 . 3.014 −11.963 76.305 1.00 43.29 . 1 243 ATOM C CD GLU D 51 . 2.464 −13.370 76.114 1.00 46.80 . 1 244 ATOM O OE1 GLU D 51 . 2.554 −13.905 74.987 1.00 50.33 . 1 245 ATOM O OE2 GLU D 51 . 1.936 −13.944 77.087 1.00 49.24 . 1 246 ATOM N N ILE D 52 . 6.266 −10.613 78.025 1.00 35.44 . 1 247 ATOM C CA ILE D 52 . 6.562 −10.361 79.430 1.00 34.77 . 1 248 ATOM C C ILE D 52 . 6.733 −8.873 79.704 1.00 35.99 . 1 249 ATOM O O ILE D 52 . 6.122 −8.325 80.625 1.00 36.84 . 1 250 ATOM C CB ILE D 52 . 7.830 −11.133 79.863 1.00 34.83 . 1 251 ATOM C CG1 ILE D 52 . 7.513 −12.632 79.898 1.00 35.31 . 1 252 ATOM C CG2 ILE D 52 . 8.322 −10.642 81.219 1.00 34.53 . 1 253 ATOM C CD1 ILE D 52 . 8.699 −13.519 80.218 1.00 34.79 . 1 254 ATOM N N ILE D 53 . 7.556 −8.211 78.901 1.00 36.24 . 1 255 ATOM C CA ILE D 53 . 7.781 −6.785 79.087 1.00 37.09 . 1 256 ATOM C C ILE D 53 . 6.479 −6.006 78.895 1.00 37.63 . 1 257 ATOM O O ILE D 53 . 6.194 −5.064 79.637 1.00 35.80 . 1 258 ATOM C CB ILE D 53 . 8.850 −6.262 78.105 1.00 37.92 . 1 259 ATOM C CG1 ILE D 53 . 10.191 −6.948 78.392 1.00 36.64 . 1 260 ATOM C CG2 ILE D 53 . 8.975 −4.747 78.222 1.00 38.39 . 1 261 ATOM C CD1 ILE D 53 . 11.353 −6.458 77.527 1.00 39.35 . 1 262 ATOM N N ALA D 54 . 5.685 −6.413 77.907 1.00 37.54 . 1 263 ATOM C CA ALA D 54 . 4.416 −5.750 77.630 1.00 39.35 . 1 264 ATOM C C ALA D 54 . 3.431 −5.871 78.793 1.00 39.75 . 1 265 ATOM O O ALA D 54 . 2.506 −5.068 78.913 1.00 39.71 . 1 266 ATOM C CB ALA D 54 . 3.787 −6.323 76.360 1.00 40.30 . 1 267 ATOM N N LYS D 55 . 3.624 −6.868 79.650 1.00 40.47 . 1 268 ATOM C CA LYS D 55 . 2.725 −7.049 80.783 1.00 41.95 . 1 269 ATOM C C LYS D 55 . 3.183 −6.379 82.083 1.00 44.09 . 1 270 ATOM O O LYS D 55 . 2.610 −6.626 83.145 1.00 43.15 . 1 271 ATOM C CB LYS D 55 . 2.474 −8.539 81.022 1.00 41.30 . 1 272 ATOM C CG LYS D 55 . 1.659 −9.197 79.920 1.00 43.17 . 1 273 ATOM C CD LYS D 55 . 1.403 −10.663 80.213 1.00 45.71 . 1 274 ATOM C CE LYS D 55 . 0.557 −11.297 79.123 1.00 47.34 . 1 275 ATOM N NZ LYS D 55 . 0.330 −12.749 79.370 1.00 48.29 . 1 276 ATOM N N ALA D 56 . 4.201 −5.526 82.001 1.00 45.20 . 1 277 ATOM C CA ALA D 56 . 4.695 −4.831 83.187 1.00 48.05 . 1 278 ATOM C C ALA D 56 . 3.499 −4.234 83.922 1.00 50.57 . 1 279 ATOM O O ALA D 56 . 2.710 −3.498 83.327 1.00 50.25 . 1 280 ATOM C CB ALA D 56 . 5.668 −3.731 82.787 1.00 46.72 . 1 281 ATOM N N THR D 57 . 3.372 −4.556 85.209 1.00 53.92 . 1 282 ATOM C CA THR D 57 . 2.256 −4.077 86.025 1.00 57.90 . 1 283 ATOM C C THR D 57 . 1.862 −2.643 85.689 1.00 59.49 . 1 284 ATOM O O THR D 57 . 0.811 −2.417 85.087 1.00 61.59 . 1 285 ATOM C CB THR D 57 . 2.568 −4.194 87.531 1.00 58.12 . 1 286 ATOM O OG1 THR D 57 . 2.788 −5.568 87.866 1.00 60.92 . 1 287 ATOM C CG2 THR D 57 . 1.408 −3.662 88.358 1.00 59.88 . 1 288 ATOM N N PRO D 58 . 2.683 −1.651 86.075 1.00 59.83 . 1 289 ATOM C CA PRO D 58 . 2.255 −0.295 85.716 1.00 59.23 . 1 290 ATOM C C PRO D 58 . 2.350 −0.197 84.194 1.00 58.68 . 1 291 ATOM O O PRO D 58 . 3.435 −0.339 83.632 1.00 59.21 . 1 292 ATOM C CB PRO D 58 . 3.287 0.594 86.412 1.00 59.69 . 1 293 ATOM C CG PRO D 58 . 3.804 −0.269 87.537 1.00 60.11 . 1 294 ATOM C CD PRO D 58 . 3.917 −1.614 86.877 1.00 59.31 . 1 295 ATOM N N PRO D 59 . 1.220 0.033 83.505 1.00 57.61 . 1 296 ATOM C CA PRO D 59 . 1.265 0.129 82.041 1.00 55.76 . 1 297 ATOM C C PRO D 59 . 2.442 0.964 81.542 1.00 54.28 . 1 298 ATOM O O PRO D 59 . 2.619 2.110 81.959 1.00 53.71 . 1 299 ATOM C CB PRO D 59 . −0.080 0.763 81.697 1.00 56.44 . 1 300 ATOM C CG PRO D 59 . −0.978 0.228 82.770 1.00 56.26 . 1 301 ATOM C CD PRO D 59 . −0.122 0.372 84.012 1.00 57.20 . 1 302 ATOM N N GLY D 60 . 3.251 0.382 80.660 1.00 52.39 . 1 303 ATOM C CA GLY D 60 . 4.391 1.099 80.116 1.00 49.44 . 1 304 ATOM C C GLY D 60 . 5.611 1.124 81.019 1.00 47.93 . 1 305 ATOM O O GLY D 60 . 6.663 1.638 80.638 1.00 47.14 . 1 306 ATOM N N ALA D 61 . 5.476 0.574 82.219 1.00 46.89 . 1 307 ATOM C CA ALA D 61 . 6.591 0.535 83.159 1.00 46.07 . 1 308 ATOM C C ALA D 61 . 7.725 −0.297 82.571 1.00 45.73 . 1 309 ATOM O O ALA D 61 . 7.482 −1.282 81.877 1.00 45.31 . 1 310 ATOM C CB ALA D 61 . 6.140 −0.070 84.483 1.00 45.78 . 1 311 ATOM N N PHE D 62 . 8.962 0.099 82.848 1.00 43.91 . 1 312 ATOM C CA PHE D 62 . 10.110 −0.641 82.349 1.00 43.18 . 1 313 ATOM C C PHE D 62 . 10.385 −1.823 83.272 1.00 42.38 . 1 314 ATOM O O PHE D 62 . 9.859 −1.884 84.386 1.00 43.65 . 1 315 ATOM C CB PHE D 62 . 11.328 0.275 82.271 1.00 45.32 . 1 316 ATOM C CG PHE D 62 . 11.077 1.550 81.514 1.00 48.14 . 1 317 ATOM C CD1 PHE D 62 . 10.422 1.528 80.285 1.00 49.14 . 1 318 ATOM C CD2 PHE D 62 . 11.505 2.773 82.022 1.00 50.21 . 1 319 ATOM C CE1 PHE D 62 . 10.197 2.706 79.571 1.00 50.36 . 1 320 ATOM C CE2 PHE D 62 . 11.286 3.960 81.314 1.00 51.00 . 1 321 ATOM C CZ PHE D 62 . 10.630 3.923 80.086 1.00 51.03 . 1 322 ATOM N N MET D 63 . 11.190 −2.771 82.806 1.00 40.21 . 1 323 ATOM C CA MET D 63 . 11.516 −3.949 83.600 1.00 38.05 . 1 324 ATOM C C MET D 63 . 13.003 −4.283 83.569 1.00 36.40 . 1 325 ATOM O O MET D 63 . 13.655 −4.187 82.531 1.00 33.49 . 1 326 ATOM C CB MET D 63 . 10.722 −5.162 83.109 1.00 39.24 . 1 327 ATOM C CG MET D 63 . 9.236 −5.107 83.416 1.00 39.73 . 1 328 ATOM S SD MET D 63 . 8.362 −6.558 82.808 1.00 40.99 . 1 329 ATOM C CE MET D 63 . 8.821 −7.805 84.025 1.00 42.19 . 1 330 ATOM N N SER D 64 . 13.537 −4.673 84.722 1.00 35.87 . 1 331 ATOM C CA SER D 64 . 14.942 −5.040 84.811 1.00 35.18 . 1 332 ATOM C C SER D 64 . 15.044 −6.506 84.413 1.00 34.56 . 1 333 ATOM O O SER D 64 . 14.046 −7.225 84.396 1.00 34.98 . 1 334 ATOM C CB SER D 64 . 15.453 −4.871 86.244 1.00 35.18 . 1 335 ATOM O OG SER D 64 . 14.931 −5.891 87.080 1.00 34.42 . 1 336 ATOM N N PRO D 65 . 16.254 −6.965 84.075 1.00 35.50 . 1 337 ATOM C CA PRO D 65 . 16.473 −8.361 83.681 1.00 35.42 . 1 338 ATOM C C PRO D 65 . 15.981 −9.338 84.757 1.00 35.33 . 1 339 ATOM O O PRO D 65 . 15.454 −10.409 84.455 1.00 34.50 . 1 340 ATOM C CB PRO D 65 . 17.986 −8.421 83.486 1.00 36.86 . 1 341 ATOM C CG PRO D 65 . 18.298 −7.045 82.961 1.00 35.94 . 1 342 ATOM C CD PRO D 65 . 17.470 −6.157 83.861 1.00 35.76 . 1 343 ATOM N N SER D 66 . 16.159 −8.956 86.017 1.00 37.68 . 1 344 ATOM C CA SER D 66 . 15.731 −9.789 87.135 1.00 38.58 . 1 345 ATOM C C SER D 66 . 14.219 −9.957 87.135 1.00 37.82 . 1 346 ATOM O O SER D 66 . 13.706 −11.059 87.351 1.00 40.08 . 1 347 ATOM C CB SER D 66 . 16.177 −9.159 88.456 1.00 39.73 . 1 348 ATOM O OG SER D 66 . 17.570 −8.903 88.438 1.00 42.78 . 1 349 ATOM N N GLU D 67 . 13.504 −8.863 86.898 1.00 36.83 . 1 350 ATOM C CA GLU D 67 . 12.050 −8.916 86.863 1.00 36.99 . 1 351 ATOM C C GLU D 67 . 11.605 −9.836 85.733 1.00 35.60 . 1 352 ATOM O O GLU D 67 . 10.754 −10.697 85.927 1.00 35.01 . 1 353 ATOM C CB GLU D 67 . 11.462 −7.521 86.646 1.00 39.07 . 1 354 ATOM C CG GLU D 67 . 11.877 −6.492 87.683 1.00 43.83 . 1 355 ATOM C CD GLU D 67 . 11.173 −5.166 87.490 1.00 45.08 . 1 356 ATOM O OE1 GLU D 67 . 10.021 −5.031 87.952 1.00 49.06 . 1 357 ATOM O OE2 GLU D 67 . 11.764 −4.261 86.863 1.00 44.84 . 1 358 ATOM N N ILE D 68 . 12.188 −9.646 84.551 1.00 35.17 . 1 359 ATOM C CA ILE D 68 . 11.850 −10.463 83.383 1.00 34.80 . 1 360 ATOM C C ILE D 68 . 12.168 −11.932 83.659 1.00 35.50 . 1 361 ATOM O O ILE D 68 . 11.390 −12.827 83.326 1.00 35.63 . 1 362 ATOM C CB ILE D 68 . 12.645 −9.989 82.144 1.00 32.18 . 1 363 ATOM C CG1 ILE D 68 . 12.332 −8.518 81.870 1.00 32.56 . 1 364 ATOM C CG2 ILE D 68 . 12.288 −10.833 80.933 1.00 32.10 . 1 365 ATOM C CD1 ILE D 68 . 13.284 −7.851 80.867 1.00 29.93 . 1 366 ATOM N N ALA D 69 . 13.321 −12.172 84.274 1.00 36.37 . 1 367 ATOM C CA ALA D 69 . 13.746 −13.525 84.608 1.00 37.05 . 1 368 ATOM C C ALA D 69 . 12.763 −14.178 85.567 1.00 37.58 . 1 369 ATOM O O ALA D 69 . 12.485 −15.370 85.465 1.00 38.90 . 1 370 ATOM C CB ALA D 69 . 15.136 −13.497 85.235 1.00 36.83 . 1 371 ATOM N N SER D 70 . 12.238 −13.392 86.499 1.00 39.91 . 1 372 ATOM C CA SER D 70 . 11.293 −13.907 87.481 1.00 41.87 . 1 373 ATOM C C SER D 70 . 9.991 −14.329 86.816 1.00 42.45 . 1 374 ATOM O O SER D 70 . 9.163 −15.004 87.429 1.00 42.35 . 1 375 ATOM C CB SER D 70 . 10.985 −12.845 88.533 1.00 42.95 . 1 376 ATOM O OG SER D 70 . 10.088 −11.877 88.015 1.00 45.66 . 1 377 ATOM N N LYS D 71 . 9.809 −13.921 85.563 1.00 41.59 . 1 378 ATOM C CA LYS D 71 . 8.599 −14.259 84.830 1.00 41.25 . 1 379 ATOM C C LYS D 71 . 8.754 −15.509 83.981 1.00 40.64 . 1 380 ATOM O O LYS D 71 . 7.776 −16.015 83.438 1.00 42.35 . 1 381 ATOM C CB LYS D 71 . 8.172 −13.081 83.950 1.00 42.18 . 1 382 ATOM C CG LYS D 71 . 7.731 −11.857 84.735 1.00 41.69 . 1 383 ATOM C CD LYS D 71 . 6.483 −12.153 85.554 1.00 45.35 . 1 384 ATOM C CE LYS D 71 . 6.008 −10.927 86.307 1.00 46.57 . 1 385 ATOM N NZ LYS D 71 . 4.731 −11.197 87.028 1.00 50.49 . 1 386 ATOM N N LEU D 72 . 9.978 −16.010 83.860 1.00 41.05 . 1 387 ATOM C CA LEU D 72 . 10.221 −17.222 83.080 1.00 42.37 . 1 388 ATOM C C LEU D 72 . 9.899 −18.436 83.948 1.00 43.44 . 1 389 ATOM O O LEU D 72 . 9.729 −18.304 85.161 1.00 43.20 . 1 390 ATOM C CB LEU D 72 . 11.681 −17.276 82.617 1.00 42.92 . 1 391 ATOM C CG LEU D 72 . 12.094 −16.276 81.532 1.00 43.27 . 1 392 ATOM C CD1 LEU D 72 . 13.582 −16.391 81.259 1.00 44.35 . 1 393 ATOM C CD2 LEU D 72 . 11.299 −16.545 80.270 1.00 46.15 . 1 394 ATOM N N PRO D 73 . 9.803 −19.635 83.343 1.00 44.80 . 1 395 ATOM C CA PRO D 73 . 9.493 −20.841 84.120 1.00 45.94 . 1 396 ATOM C C PRO D 73 . 10.450 −21.028 85.289 1.00 46.39 . 1 397 ATOM O O PRO D 73 . 11.652 −20.794 85.162 1.00 46.11 . 1 398 ATOM C CB PRO D 73 . 9.614 −21.958 83.087 1.00 44.82 . 1 399 ATOM C CG PRO D 73 . 9.172 −21.286 81.834 1.00 45.63 . 1 400 ATOM C CD PRO D 73 . 9.903 −19.958 81.910 1.00 45.26 . 1 401 ATOM N N ALA D 74 . 9.906 −21.448 86.428 1.00 47.17 . 1 402 ATOM C CA ALA D 74 . 10.705 −21.661 87.631 1.00 47.49 . 1 403 ATOM C C ALA D 74 . 11.948 −22.499 87.351 1.00 48.19 . 1 404 ATOM O O ALA D 74 . 13.036 −22.196 87.841 1.00 48.10 . 1 405 ATOM C CB ALA D 74 . 9.856 −22.337 88.702 1.00 49.32 . 1 406 ATOM N N SER D 75 . 11.775 −23.547 86.552 1.00 48.40 . 1 407 ATOM C CA SER D 75 . 12.858 −24.458 86.200 1.00 50.53 . 1 408 ATOM C C SER D 75 . 13.999 −23.836 85.393 1.00 51.92 . 1 409 ATOM O O SER D 75 . 15.007 −24.493 85.137 1.00 52.82 . 1 410 ATOM C CB SER D 75 . 12.289 −25.643 85.423 1.00 50.74 . 1 411 ATOM O OG SER D 75 . 11.637 −25.201 84.244 1.00 52.51 . 1 412 ATOM N N THR D 76 . 13.852 −22.577 84.995 1.00 52.78 . 1 413 ATOM C CA THR D 76 . 14.883 −21.916 84.201 1.00 52.43 . 1 414 ATOM C C THR D 76 . 15.615 −20.842 84.989 1.00 53.38 . 1 415 ATOM O O THR D 76 . 16.583 −20.258 84.503 1.00 53.76 . 1 416 ATOM C CB THR D 76 . 14.274 −21.221 82.961 1.00 52.82 . 1 417 ATOM O OG1 THR D 76 . 13.442 −20.134 83.389 1.00 50.05 . 1 418 ATOM C CG2 THR D 76 . 13.442 −22.198 82.144 1.00 50.97 . 1 419 ATOM N N GLN D 77 . 15.169 −20.588 86.211 1.00 53.87 . 1 420 ATOM C CA GLN D 77 . 15.777 −19.528 86.997 1.00 55.05 . 1 421 ATOM C C GLN D 77 . 17.016 −19.845 87.825 1.00 54.81 . 1 422 ATOM O O GLN D 77 . 16.929 −20.061 89.034 1.00 56.57 . 1 423 ATOM C CB GLN D 77 . 14.709 −18.882 87.881 1.00 55.93 . 1 424 ATOM C CG GLN D 77 . 13.577 −18.265 87.075 1.00 57.60 . 1 425 ATOM C CD GLN D 77 . 12.603 −17.494 87.930 1.00 59.76 . 1 426 ATOM O OE1 GLN D 77 . 12.999 −16.625 88.707 1.00 61.33 . 1 427 ATOM N NE2 GLN D 77 . 11.316 −17.799 87.786 1.00 59.86 . 1 428 ATOM N N HIS D 78 . 18.174 −19.857 87.169 1.00 53.29 . 1 429 ATOM C CA HIS D 78 . 19.433 −20.098 87.861 1.00 51.54 . 1 430 ATOM C C HIS D 78 . 20.041 −18.747 88.232 1.00 49.45 . 1 431 ATOM O O HIS D 78 . 19.553 −17.700 87.810 1.00 48.37 . 1 432 ATOM C CB HIS D 78 . 20.399 −20.900 86.984 1.00 53.61 . 1 433 ATOM C CG HIS D 78 . 20.550 −20.361 85.598 1.00 54.99 . 1 434 ATOM N ND1 HIS D 78 . 19.567 −20.488 84.639 1.00 56.64 . 1 435 ATOM C CD2 HIS D 78 . 21.569 −19.693 85.007 1.00 55.50 . 1 436 ATOM C CE1 HIS D 78 . 19.976 −19.923 83.517 1.00 56.60 . 1 437 ATOM N NE2 HIS D 78 . 21.187 −19.433 83.713 1.00 56.06 . 1 438 ATOM N N SER D 79 . 21.109 −18.772 89.019 1.00 47.55 . 1 439 ATOM C CA SER D 79 . 21.748 −17.544 89.479 1.00 45.84 . 1 440 ATOM C C SER D 79 . 22.164 −16.559 88.399 1.00 44.34 . 1 441 ATOM O O SER D 79 . 22.107 −15.347 88.609 1.00 45.47 . 1 442 ATOM C CB SER D 79 . 22.970 −17.881 90.344 1.00 45.55 . 1 443 ATOM O OG SER D 79 . 23.867 −18.739 89.660 1.00 46.23 . 1 444 ATOM N N ASP D 80 . 22.571 −17.073 87.245 1.00 42.67 . 1 445 ATOM C CA ASP D 80 . 23.039 −16.219 86.161 1.00 42.23 . 1 446 ATOM C C ASP D 80 . 21.992 −15.866 85.102 1.00 41.49 . 1 447 ATOM O O ASP D 80 . 22.323 −15.245 84.096 1.00 41.46 . 1 448 ATOM C CB ASP D 80 . 24.250 −16.880 85.492 1.00 42.76 . 1 449 ATOM C CG ASP D 80 . 25.018 −15.930 84.594 1.00 44.40 . 1 450 ATOM O OD1 ASP D 80 . 25.389 −14.835 85.064 1.00 44.96 . 1 451 ATOM O OD2 ASP D 80 . 25.259 −16.279 83.421 1.00 45.64 . 1 452 ATOM N N LEU D 81 . 20.735 −16.237 85.331 1.00 40.40 . 1 453 ATOM C CA LEU D 81 . 19.681 −15.958 84.357 1.00 39.88 . 1 454 ATOM C C LEU D 81 . 19.521 −14.473 84.016 1.00 40.15 . 1 455 ATOM O O LEU D 81 . 19.530 −14.099 82.843 1.00 38.35 . 1 456 ATOM C CB LEU D 81 . 18.343 −16.527 84.840 1.00 41.22 . 1 457 ATOM C CG LEU D 81 . 17.160 −16.342 83.879 1.00 41.89 . 1 458 ATOM C CD1 LEU D 81 . 17.470 −17.010 82.545 1.00 42.42 . 1 459 ATOM C CD2 LEU D 81 . 15.896 −16.931 84.487 1.00 40.60 . 1 460 ATOM N N PRO D 82 . 19.369 −13.606 85.032 1.00 40.04 . 1 461 ATOM C CA PRO D 82 . 19.213 −12.173 84.757 1.00 39.95 . 1 462 ATOM C C PRO D 82 . 20.346 −11.601 83.903 1.00 41.09 . 1 463 ATOM O O PRO D 82 . 20.118 −10.813 82.979 1.00 39.75 . 1 464 ATOM C CB PRO D 82 . 19.176 −11.557 86.155 1.00 40.21 . 1 465 ATOM C CG PRO D 82 . 18.517 −12.636 86.970 1.00 39.60 . 1 466 ATOM C CD PRO D 82 . 19.232 −13.879 86.475 1.00 40.92 . 1 467 ATOM N N ASN D 83 . 21.569 −12.003 84.221 1.00 40.75 . 1 468 ATOM C CA ASN D 83 . 22.746 −11.534 83.500 1.00 41.81 . 1 469 ATOM C C ASN D 83 . 22.670 −11.911 82.024 1.00 39.17 . 1 470 ATOM O O ASN D 83 . 22.938 −11.091 81.146 1.00 36.90 . 1 471 ATOM C CB ASN D 83 . 23.998 −12.139 84.137 1.00 44.59 . 1 472 ATOM C CG ASN D 83 . 24.102 −11.817 85.622 1.00 50.24 . 1 473 ATOM O OD1 ASN D 83 . 24.479 −10.705 86.004 1.00 53.16 . 1 474 ATOM N ND2 ASN D 83 . 23.743 −12.782 86.466 1.00 51.39 . 1 475 ATOM N N ARG D 84 . 22.290 −13.157 81.766 1.00 37.15 . 1 476 ATOM C CA ARG D 84 . 22.184 −13.665 80.406 1.00 35.22 . 1 477 ATOM C C ARG D 84 . 21.095 −12.963 79.615 1.00 34.26 . 1 478 ATOM O O ARG D 84 . 21.284 −12.647 78.444 1.00 32.03 . 1 479 ATOM C CB ARG D 84 . 21.922 −15.165 80.441 1.00 37.24 . 1 480 ATOM C CG ARG D 84 . 23.061 −15.927 81.082 1.00 38.68 . 1 481 ATOM C CD ARG D 84 . 22.826 −17.413 81.078 1.00 41.36 . 1 482 ATOM N NE ARG D 84 . 23.927 −18.104 81.737 1.00 44.29 . 1 483 ATOM C CZ ARG D 84 . 24.044 −19.424 81.808 1.00 43.97 . 1 484 ATOM N NH1 ARG D 84 . 23.124 −20.206 81.260 1.00 43.52 . 1 485 ATOM N NH2 ARG D 84 . 25.088 −19.957 82.422 1.00 45.14 . 1 486 ATOM N N LEU D 85 . 19.955 −12.715 80.255 1.00 33.02 . 1 487 ATOM C CA LEU D 85 . 18.862 −12.032 79.579 1.00 31.76 . 1 488 ATOM C C LEU D 85 . 19.302 −10.620 79.236 1.00 31.44 . 1 489 ATOM O O LEU D 85 . 19.036 −10.130 78.142 1.00 32.23 . 1 490 ATOM C CB LEU D 85 . 17.615 −11.991 80.463 1.00 31.80 . 1 491 ATOM C CG LEU D 85 . 16.891 −13.320 80.700 1.00 32.04 . 1 492 ATOM C CD1 LEU D 85 . 15.666 −13.072 81.561 1.00 32.66 . 1 493 ATOM C CD2 LEU D 85 . 16.491 −13.944 79.360 1.00 30.42 . 1 494 ATOM N N ASP D 86 . 20.000 −9.980 80.170 1.00 30.34 . 1 495 ATOM C CA ASP D 86 . 20.483 −8.619 79.973 1.00 31.39 . 1 496 ATOM C C ASP D 86 . 21.388 −8.524 78.745 1.00 31.13 . 1 497 ATOM O O ASP D 86 . 21.334 −7.543 77.993 1.00 30.27 . 1 498 ATOM C CB ASP D 86 . 21.238 −8.144 81.219 1.00 32.88 . 1 499 ATOM C CG ASP D 86 . 21.623 −6.673 81.150 1.00 32.55 . 1 500 ATOM O OD1 ASP D 86 . 20.774 −5.843 80.774 1.00 34.93 . 1 501 ATOM O OD2 ASP D 86 . 22.773 −6.340 81.487 1.00 37.20 . 1 502 ATOM N N ARG D 87 . 22.220 −9.539 78.543 1.00 28.81 . 1 503 ATOM C CA ARG D 87 . 23.123 −9.548 77.400 1.00 30.69 . 1 504 ATOM C C ARG D 87 . 22.326 −9.595 76.092 1.00 28.68 . 1 505 ATOM O O ARG D 87 . 22.719 −8.989 75.099 1.00 28.70 . 1 506 ATOM C CB ARG D 87 . 24.086 −10.736 77.504 1.00 33.93 . 1 507 ATOM C CG ARG D 87 . 24.937 −10.678 78.763 1.00 39.19 . 1 508 ATOM C CD ARG D 87 . 25.756 −11.939 78.973 1.00 43.58 . 1 509 ATOM N NE ARG D 87 . 26.860 −12.064 78.028 1.00 46.15 . 1 510 ATOM C CZ ARG D 87 . 27.689 −13.101 78.003 1.00 48.10 . 1 511 ATOM N NH1 ARG D 87 . 27.527 −14.092 78.869 1.00 48.50 . 1 512 ATOM N NH2 ARG D 87 . 28.676 −13.153 77.118 1.00 49.31 . 1 513 ATOM N N MET D 88 . 21.204 −10.303 76.102 1.00 29.42 . 1 514 ATOM C CA MET D 88 . 20.346 −10.392 74.920 1.00 29.58 . 1 515 ATOM C C MET D 88 . 19.578 −9.080 74.764 1.00 29.67 . 1 516 ATOM O O MET D 88 . 19.472 −8.522 73.675 1.00 26.68 . 1 517 ATOM C CB MET D 88 . 19.326 −11.516 75.077 1.00 29.34 . 1 518 ATOM C CG MET D 88 . 19.890 −12.920 75.142 1.00 30.56 . 1 519 ATOM S SD MET D 88 . 18.585 −14.085 75.574 1.00 33.80 . 1 520 ATOM C CE MET D 88 . 17.454 −13.896 74.164 1.00 34.39 . 1 521 ATOM N N LEU D 89 . 19.035 −8.601 75.875 1.00 29.81 . 1 522 ATOM C CA LEU D 89 . 18.256 −7.373 75.881 1.00 29.37 . 1 523 ATOM C C LEU D 89 . 19.079 −6.205 75.350 1.00 28.58 . 1 524 ATOM O O LEU D 89 . 18.560 −5.368 74.617 1.00 27.85 . 1 525 ATOM C CB LEU D 89 . 17.734 −7.112 77.298 1.00 28.96 . 1 526 ATOM C CG LEU D 89 . 16.766 −8.199 77.785 1.00 27.87 . 1 527 ATOM C CD1 LEU D 89 . 16.540 −8.071 79.285 1.00 24.75 . 1 528 ATOM C CD2 LEU D 89 . 15.437 −8.086 77.039 1.00 26.57 . 1 529 ATOM N N ARG D 90 . 20.364 −6.158 75.705 1.00 27.99 . 1 530 ATOM C CA ARG D 90 . 21.261 −5.112 75.214 1.00 27.95 . 1 531 ATOM C C ARG D 90 . 21.262 −5.109 73.675 1.00 29.22 . 1 532 ATOM O O ARG D 90 . 21.190 −4.053 73.048 1.00 28.67 . 1 533 ATOM C CB ARG D 90 . 22.696 −5.359 75.688 1.00 29.54 . 1 534 ATOM C CG ARG D 90 . 23.176 −4.565 76.908 1.00 31.29 . 1 535 ATOM C CD ARG D 90 . 24.620 −4.988 77.211 1.00 34.06 . 1 536 ATOM N NE ARG D 90 . 25.260 −4.258 78.306 1.00 35.04 . 1 537 ATOM C CZ ARG D 90 . 25.830 −3.060 78.195 1.00 34.34 . 1 538 ATOM N NH1 ARG D 90 . 25.853 −2.423 77.030 1.00 33.42 . 1 539 ATOM N NH2 ARG D 90 . 26.390 −2.499 79.259 1.00 33.86 . 1 540 ATOM N N LEU D 91 . 21.356 −6.293 73.070 1.00 28.32 . 1 541 ATOM C CA LEU D 91 . 21.372 −6.394 71.602 1.00 28.14 . 1 542 ATOM C C LEU D 91 . 20.051 −5.904 71.005 1.00 27.46 . 1 543 ATOM O O LEU D 91 . 20.043 −5.151 70.027 1.00 26.56 . 1 544 ATOM C CB LEU D 91 . 21.604 −7.846 71.157 1.00 28.87 . 1 545 ATOM C CG LEU D 91 . 22.588 −8.176 70.023 1.00 31.48 . 1 546 ATOM C CD1 LEU D 91 . 22.026 −9.342 69.220 1.00 27.00 . 1 547 ATOM C CD2 LEU D 91 . 22.848 −6.969 69.127 1.00 25.44 . 1 548 ATOM N N LEU D 92 . 18.939 −6.338 71.593 1.00 25.94 . 1 549 ATOM C CA LEU D 92 . 17.620 −5.941 71.117 1.00 28.35 . 1 550 ATOM C C LEU D 92 . 17.434 −4.424 71.222 1.00 29.46 . 1 551 ATOM O O LEU D 92 . 16.817 −3.801 70.353 1.00 28.29 . 1 552 ATOM C CB LEU D 92 . 16.539 −6.681 71.907 1.00 28.70 . 1 553 ATOM C CG LEU D 92 . 16.584 −8.207 71.757 1.00 30.45 . 1 554 ATOM C CD1 LEU D 92 . 15.630 −8.847 72.739 1.00 29.69 . 1 555 ATOM C CD2 LEU D 92 . 16.226 −8.601 70.324 1.00 26.52 . 1 556 ATOM N N ALA D 93 . 17.980 −3.829 72.280 1.00 29.26 . 1 557 ATOM C CA ALA D 93 . 17.892 −2.384 72.459 1.00 29.59 . 1 558 ATOM C C ALA D 93 . 18.752 −1.698 71.399 1.00 28.85 . 1 559 ATOM O O ALA D 93 . 18.374 −0.663 70.854 1.00 27.13 . 1 560 ATOM C CB ALA D 93 . 18.367 −1.987 73.867 1.00 29.35 . 1 561 ATOM N N SER D 94 . 19.910 −2.282 71.101 1.00 29.13 . 1 562 ATOM C CA SER D 94 . 20.800 −1.716 70.097 1.00 28.23 . 1 563 ATOM C C SER D 94 . 20.136 −1.756 68.724 1.00 28.29 . 1 564 ATOM O O SER D 94 . 20.452 −0.947 67.850 1.00 28.03 . 1 565 ATOM C CB SER D 94 . 22.120 −2.487 70.053 1.00 28.16 . 1 566 ATOM O OG SER D 94 . 22.777 −2.424 71.309 1.00 27.31 . 1 567 ATOM N N TYR D 95 . 19.211 −2.693 68.538 1.00 28.27 . 1 568 ATOM C CA TYR D 95 . 18.509 −2.806 67.263 1.00 29.52 . 1 569 ATOM C C TYR D 95 . 17.163 −2.075 67.243 1.00 30.19 . 1 570 ATOM O O TYR D 95 . 16.328 −2.319 66.373 1.00 29.35 . 1 571 ATOM C CB TYR D 95 . 18.334 −4.283 66.872 1.00 29.26 . 1 572 ATOM C CG TYR D 95 . 19.511 −4.821 66.082 1.00 28.84 . 1 573 ATOM C CD1 TYR D 95 . 20.682 −5.235 66.716 1.00 27.50 . 1 574 ATOM C CD2 TYR D 95 . 19.477 −4.857 64.690 1.00 30.47 . 1 575 ATOM C CE1 TYR D 95 . 21.790 −5.666 65.982 1.00 26.49 . 1 576 ATOM C CE2 TYR D 95 . 20.576 −5.283 63.947 1.00 28.69 . 1 577 ATOM C CZ TYR D 95 . 21.728 −5.684 64.596 1.00 29.78 . 1 578 ATOM O OH TYR D 95 . 22.810 −6.094 63.849 1.00 30.85 . 1 579 ATOM N N SER D 96 . 16.969 −1.178 68.212 1.00 32.95 . 1 580 ATOM C CA SER D 96 . 15.763 −0.353 68.323 1.00 32.96 . 1 581 ATOM C C SER D 96 . 14.456 −1.034 68.673 1.00 32.65 . 1 582 ATOM O O SER D 96 . 13.407 −0.390 68.644 1.00 32.15 . 1 583 ATOM C CB SER D 96 . 15.548 0.446 67.037 1.00 34.56 . 1 584 ATOM O OG SER D 96 . 16.631 1.323 66.808 1.00 41.24 . 1 585 ATOM N N VAL D 97 . 14.496 −2.320 69.004 1.00 31.19 . 1 586 ATOM C CA VAL D 97 . 13.271 −3.034 69.356 1.00 30.81 . 1 587 ATOM C C VAL D 97 . 12.863 −2.743 70.806 1.00 30.67 . 1 588 ATOM O O VAL D 97 . 11.683 −2.776 71.165 1.00 28.95 . 1 589 ATOM C CB VAL D 97 . 13.448 −4.557 69.162 1.00 32.93 . 1 590 ATOM C CG1 VAL D 97 . 12.277 −5.297 69.757 1.00 37.64 . 1 591 ATOM C CG2 VAL D 97 . 13.560 −4.870 67.677 1.00 35.18 . 1 592 ATOM N N LEU D 98 . 13.851 −2.449 71.636 1.00 31.19 . 1 593 ATOM C CA LEU D 98 . 13.584 −2.144 73.031 1.00 32.14 . 1 594 ATOM C C LEU D 98 . 14.161 −0.784 73.370 1.00 31.21 . 1 595 ATOM O O LEU D 98 . 15.066 −0.298 72.692 1.00 29.93 . 1 596 ATOM C CB LEU D 98 . 14.218 −3.204 73.941 1.00 30.54 . 1 597 ATOM C CG LEU D 98 . 13.779 −4.652 73.720 1.00 31.31 . 1 598 ATOM C CD1 LEU D 98 . 14.532 −5.570 74.681 1.00 30.19 . 1 599 ATOM C CD2 LEU D 98 . 12.287 −4.775 73.935 1.00 29.32 . 1 600 ATOM N N THR D 99 . 13.605 −0.171 74.408 1.00 32.67 . 1 601 ATOM C CA THR D 99 . 14.077 1.116 74.901 1.00 33.92 . 1 602 ATOM C C THR D 99 . 14.840 0.754 76.170 1.00 33.68 . 1 603 ATOM O O THR D 99 . 14.592 −0.291 76.767 1.00 31.41 . 1 604 ATOM C CB THR D 99 . 12.906 2.059 75.280 1.00 33.82 . 1 605 ATOM O OG1 THR D 99 . 12.124 1.464 76.320 1.00 33.29 . 1 606 ATOM C CG2 THR D 99 . 12.017 2.313 74.076 1.00 33.42 . 1 607 ATOM N N SER D 100 . 15.767 1.605 76.584 1.00 35.21 . 1 608 ATOM C CA SER D 100 . 16.529 1.312 77.784 1.00 38.82 . 1 609 ATOM C C SER D 100 . 16.839 2.555 78.599 1.00 38.65 . 1 610 ATOM O O SER D 100 . 16.949 3.657 78.066 1.00 38.62 . 1 611 ATOM C CB SER D 100 . 17.836 0.610 77.416 1.00 38.72 . 1 612 ATOM O OG SER D 100 . 18.534 0.204 78.575 1.00 42.94 . 1 613 ATOM N N THR D 101 . 16.978 2.355 79.903 1.00 39.42 . 1 614 ATOM C CA THR D 101 . 17.307 3.427 80.826 1.00 39.89 . 1 615 ATOM C C THR D 101 . 17.712 2.765 82.135 1.00 40.44 . 1 616 ATOM O O THR D 101 . 17.848 1.540 82.202 1.00 39.34 . 1 617 ATOM C CB THR D 101 . 16.095 4.381 81.057 1.00 40.30 . 1 618 ATOM O OG1 THR D 101 . 16.528 5.532 81.789 1.00 42.10 . 1 619 ATOM C CG2 THR D 101 . 14.991 3.686 81.834 1.00 39.35 . 1 620 ATOM N N THR D 102 . 17.918 3.569 83.170 1.00 41.42 . 1 621 ATOM C CA THR D 102 . 18.299 3.032 84.472 1.00 43.16 . 1 622 ATOM C C THR D 102 . 17.409 3.646 85.540 1.00 43.95 . 1 623 ATOM O O THR D 102 . 17.054 4.821 85.453 1.00 44.76 . 1 624 ATOM C CB THR D 102 . 19.767 3.361 84.811 1.00 44.12 . 1 625 ATOM O OG1 THR D 102 . 19.968 4.778 84.735 1.00 45.33 . 1 626 ATOM C CG2 THR D 102 . 20.712 2.672 83.837 1.00 44.77 . 1 627 ATOM N N ARG D 103 . 17.031 2.847 86.530 1.00 44.59 . 1 628 ATOM C CA ARG D 103 . 16.196 3.344 87.614 1.00 46.01 . 1 629 ATOM C C ARG D 103 . 16.957 3.142 88.912 1.00 46.50 . 1 630 ATOM O O ARG D 103 . 17.696 2.167 89.065 1.00 46.56 . 1 631 ATOM C CB ARG D 103 . 14.858 2.604 87.664 1.00 46.73 . 1 632 ATOM C CG ARG D 103 . 14.938 1.187 88.172 1.00 46.55 . 1 633 ATOM C CD ARG D 103 . 13.576 0.520 88.120 1.00 48.40 . 1 634 ATOM N NE ARG D 103 . 13.650 −0.863 88.573 1.00 49.47 . 1 635 ATOM C CZ ARG D 103 . 12.742 −1.792 88.301 1.00 48.80 . 1 636 ATOM N NH1 ARG D 103 . 11.676 −1.492 87.573 1.00 49.04 . 1 637 ATOM N NH2 ARG D 103 . 12.912 −3.027 88.752 1.00 48.52 . 1 638 ATOM N N THR D 104 . 16.780 4.066 89.847 1.00 47.24 . 1 639 ATOM C CA THR D 104 . 17.484 3.983 91.116 1.00 46.43 . 1 640 ATOM C C THR D 104 . 16.784 3.139 92.162 1.00 46.21 . 1 641 ATOM O O THR D 104 . 15.558 3.142 92.276 1.00 46.51 . 1 642 ATOM C CB THR D 104 . 17.743 5.376 91.682 1.00 46.36 . 1 643 ATOM O OG1 THR D 104 . 18.507 6.124 90.733 1.00 46.04 . 1 644 ATOM C CG2 THR D 104 . 18.523 5.285 92.988 1.00 47.73 . 1 645 ATOM N N ILE D 105 . 17.598 2.412 92.919 1.00 45.96 . 1 646 ATOM C CA ILE D 105 . 17.141 1.529 93.980 1.00 45.79 . 1 647 ATOM C C ILE D 105 . 17.001 2.305 95.292 1.00 45.31 . 1 648 ATOM O O ILE D 105 . 17.477 3.430 95.416 1.00 43.95 . 1 649 ATOM C CB ILE D 105 . 18.155 0.381 94.203 1.00 46.03 . 1 650 ATOM C CG1 ILE D 105 . 18.694 −0.109 92.855 1.00 47.78 . 1 651 ATOM C CG2 ILE D 105 . 17.499 −0.757 94.967 1.00 47.73 . 1 652 ATOM C CD1 ILE D 105 . 17.627 −0.524 91.860 1.00 46.46 . 1 653 ATOM N N GLU D 106 . 16.352 1.674 96.262 1.00 45.36 . 1 654 ATOM C CA GLU D 106 . 16.118 2.242 97.585 1.00 45.20 . 1 655 ATOM C C GLU D 106 . 17.399 2.726 98.268 1.00 44.43 . 1 656 ATOM O O GLU D 106 . 17.394 3.728 98.986 1.00 43.82 . 1 657 ATOM C CB GLU D 106 . 15.431 1.184 98.449 1.00 46.99 . 1 658 ATOM C CG GLU D 106 . 15.271 1.536 99.902 1.00 49.04 . 1 659 ATOM C CD GLU D 106 . 14.632 0.407 100.693 1.00 49.55 . 1 660 ATOM O OE1 GLU D 106 . 13.514 −0.010 100.329 1.00 49.23 . 1 661 ATOM O OE2 GLU D 106 . 15.247 −0.060 101.676 1.00 49.60 . 1 662 ATOM N N ASP D 107 . 18.496 2.013 98.044 1.00 43.37 . 1 663 ATOM C CA ASP D 107 . 19.771 2.370 98.654 1.00 42.78 . 1 664 ATOM C C ASP D 107 . 20.596 3.280 97.759 1.00 41.64 . 1 665 ATOM O O ASP D 107 . 21.790 3.458 97.977 1.00 41.89 . 1 666 ATOM C CB ASP D 107 . 20.564 1.103 98.985 1.00 43.74 . 1 667 ATOM C CG ASP D 107 . 20.868 0.267 97.756 1.00 43.93 . 1 668 ATOM O OD1 ASP D 107 . 21.298 −0.892 97.924 1.00 43.45 . 1 669 ATOM O OD2 ASP D 107 . 20.685 0.773 96.627 1.00 41.79 . 1 670 ATOM N N GLY D 108 . 19.954 3.855 96.750 1.00 40.78 . 1 671 ATOM C CA GLY D 108 . 20.664 4.746 95.851 1.00 40.98 . 1 672 ATOM C C GLY D 108 . 21.352 4.008 94.722 1.00 42.61 . 1 673 ATOM O O GLY D 108 . 21.996 4.619 93.869 1.00 43.39 . 1 674 ATOM N N GLY D 109 . 21.224 2.686 94.722 1.00 42.76 . 1 675 ATOM C CA GLY D 109 . 21.837 1.892 93.673 1.00 43.41 . 1 676 ATOM C C GLY D 109 . 21.117 2.101 92.354 1.00 42.79 . 1 677 ATOM O O GLY D 109 . 19.997 2.607 92.324 1.00 41.74 . 1 678 ATOM N N ALA D 110 . 21.755 1.712 91.256 1.00 42.61 . 1 679 ATOM C CA ALA D 110 . 21.149 1.879 89.941 1.00 43.23 . 1 680 ATOM C C ALA D 110 . 21.081 0.552 89.195 1.00 42.23 . 1 681 ATOM O O ALA D 110 . 21.962 −0.292 89.331 1.00 42.84 . 1 682 ATOM C CB ALA D 110 . 21.943 2.901 89.129 1.00 41.77 . 1 683 ATOM N N GLU D 111 . 20.026 0.369 88.412 1.00 42.14 . 1 684 ATOM C CA GLU D 111 . 19.874 −0.857 87.645 1.00 41.07 . 1 685 ATOM C C GLU D 111 . 19.295 −0.541 86.277 1.00 40.13 . 1 686 ATOM O O GLU D 111 . 18.469 0.359 86.133 1.00 39.75 . 1 687 ATOM C CB GLU D 111 . 18.970 −1.849 88.387 1.00 41.97 . 1 688 ATOM C CG GLU D 111 . 17.507 −1.456 88.467 1.00 44.71 . 1 689 ATOM C CD GLU D 111 . 16.694 −2.422 89.317 1.00 47.11 . 1 690 ATOM O OE1 GLU D 111 . 16.944 −3.646 89.246 1.00 50.64 . 1 691 ATOM O OE2 GLU D 111 . 15.795 −1.961 90.049 1.00 49.04 . 1 692 ATOM N N ARG D 112 . 19.744 −1.277 85.267 1.00 38.73 . 1 693 ATOM C CA ARG D 112 . 19.252 −1.069 83.911 1.00 36.78 . 1 694 ATOM C C ARG D 112 . 17.881 −1.711 83.739 1.00 35.65 . 1 695 ATOM O O ARG D 112 . 17.631 −2.812 84.222 1.00 34.47 . 1 696 ATOM C CB ARG D 112 . 20.243 −1.655 82.898 1.00 38.00 . 1 697 ATOM C CG ARG D 112 . 19.748 −1.662 81.456 1.00 35.48 . 1 698 ATOM C CD ARG D 112 . 20.911 −1.784 80.477 1.00 36.95 . 1 699 ATOM N NE ARG D 112 . 21.813 −2.892 80.795 1.00 38.82 . 1 700 ATOM C CZ ARG D 112 . 23.087 −2.741 81.146 1.00 38.42 . 1 701 ATOM N NH1 ARG D 112 . 23.615 −1.526 81.231 1.00 38.36 . 1 702 ATOM N NH2 ARG D 112 . 23.838 −3.804 81.394 1.00 36.70 . 1 703 ATOM N N VAL D 113 . 16.983 −1.007 83.065 1.00 34.85 . 1 704 ATOM C CA VAL D 113 . 15.647 −1.530 82.826 1.00 34.78 . 1 705 ATOM C C VAL D 113 . 15.309 −1.337 81.356 1.00 33.25 . 1 706 ATOM O O VAL D 113 . 15.876 −0.470 80.692 1.00 33.02 . 1 707 ATOM C CB VAL D 113 . 14.586 −0.815 83.689 1.00 35.42 . 1 708 ATOM C CG1 VAL D 113 . 14.825 −1.123 85.165 1.00 37.82 . 1 709 ATOM C CG2 VAL D 113 . 14.629 0.685 83.430 1.00 37.07 . 1 710 ATOM N N TYR D 114 . 14.383 −2.148 80.857 1.00 33.98 . 1 711 ATOM C CA TYR D 114 . 13.997 −2.078 79.454 1.00 31.63 . 1 712 ATOM C C TYR D 114 . 12.503 −1.913 79.237 1.00 31.59 . 1 713 ATOM O O TYR D 114 . 11.691 −2.264 80.095 1.00 31.74 . 1 714 ATOM C CB TYR D 114 . 14.448 −3.342 78.725 1.00 32.26 . 1 715 ATOM C CG TYR D 114 . 15.935 −3.605 78.742 1.00 31.28 . 1 716 ATOM C CD1 TYR D 114 . 16.547 −4.230 79.831 1.00 32.63 . 1 717 ATOM C CD2 TYR D 114 . 16.727 −3.269 77.646 1.00 32.58 . 1 718 ATOM C CE1 TYR D 114 . 17.913 −4.521 79.818 1.00 31.40 . 1 719 ATOM C CE2 TYR D 114 . 18.090 −3.556 77.622 1.00 30.76 . 1 720 ATOM C CZ TYR D 114 . 18.674 −4.184 78.707 1.00 30.81 . 1 721 ATOM O OH TYR D 114 . 20.007 −4.505 78.657 1.00 29.06 . 1 722 ATOM N N GLY D 115 . 12.163 −1.394 78.061 1.00 30.99 . 1 723 ATOM C CA GLY D 115 . 10.777 −1.192 77.676 1.00 32.40 . 1 724 ATOM C C GLY D 115 . 10.637 −1.475 76.188 1.00 32.28 . 1 725 ATOM O O GLY D 115 . 11.633 −1.692 75.493 1.00 32.11 . 1 726 ATOM N N LEU D 116 . 9.407 −1.491 75.691 1.00 32.99 . 1 727 ATOM C CA LEU D 116 . 9.166 −1.747 74.275 1.00 33.44 . 1 728 ATOM C C LEU D 116 . 9.136 −0.429 73.516 1.00 33.78 . 1 729 ATOM O O LEU D 116 . 8.521 0.534 73.968 1.00 33.06 . 1 730 ATOM C CB LEU D 116 . 7.829 −2.464 74.087 1.00 32.86 . 1 731 ATOM C CG LEU D 116 . 7.699 −3.849 74.722 1.00 35.68 . 1 732 ATOM C CD1 LEU D 116 . 6.243 −4.277 74.718 1.00 35.39 . 1 733 ATOM C CD2 LEU D 116 . 8.570 −4.849 73.962 1.00 34.76 . 1 734 ATOM N N SER D 117 . 9.808 −0.380 72.371 1.00 32.26 . 1 735 ATOM C CA SER D 117 . 9.808 0.832 71.563 1.00 31.81 . 1 736 ATOM C C SER D 117 . 8.572 0.789 70.671 1.00 31.04 . 1 737 ATOM O O SER D 117 . 7.827 −0.192 70.679 1.00 29.84 . 1 738 ATOM C CB SER D 117 . 11.063 0.903 70.694 1.00 32.53 . 1 739 ATOM O OG SER D 117 . 11.039 −0.098 69.690 1.00 32.21 . 1 740 ATOM N N MET D 118 . 8.357 1.851 69.904 1.00 30.39 . 1 741 ATOM C CA MET D 118 . 7.213 1.927 69.005 1.00 30.95 . 1 742 ATOM C C MET D 118 . 7.329 0.778 67.999 1.00 30.37 . 1 743 ATOM O O MET D 118 . 6.330 0.236 67.526 1.00 32.50 . 1 744 ATOM C CB MET D 118 . 7.227 3.272 68.274 1.00 33.19 . 1 745 ATOM C CG MET D 118 . 5.889 3.697 67.704 1.00 38.06 . 1 746 ATOM S SD MET D 118 . 6.045 5.291 66.877 1.00 41.19 . 1 747 ATOM C CE MET D 118 . 4.651 5.213 65.744 1.00 41.26 . 1 748 ATOM N N VAL D 119 . 8.565 0.421 67.679 1.00 28.19 . 1 749 ATOM C CA VAL D 119 . 8.844 −0.672 66.754 1.00 27.98 . 1 750 ATOM C C VAL D 119 . 8.662 −2.007 67.482 1.00 28.96 . 1 751 ATOM O O VAL D 119 . 8.059 −2.947 66.955 1.00 27.46 . 1 752 ATOM C CB VAL D 119 . 10.284 −0.565 66.227 1.00 28.04 . 1 753 ATOM C CG1 VAL D 119 . 10.648 −1.792 65.406 1.00 26.75 . 1 754 ATOM C CG2 VAL D 119 . 10.423 0.709 65.394 1.00 26.69 . 1 755 ATOM N N GLY D 120 . 9.180 −2.076 68.705 1.00 27.17 . 1 756 ATOM C CA GLY D 120 . 9.074 −3.294 69.488 1.00 27.26 . 1 757 ATOM C C GLY D 120 . 7.675 −3.783 69.815 1.00 26.91 . 1 758 ATOM O O GLY D 120 . 7.478 −4.978 70.049 1.00 26.33 . 1 759 ATOM N N LYS D 121 . 6.693 −2.887 69.851 1.00 25.79 . 1 760 ATOM C CA LYS D 121 . 5.343 −3.314 70.180 1.00 26.31 . 1 761 ATOM C C LYS D 121 . 4.815 −4.325 69.169 1.00 26.05 . 1 762 ATOM O O LYS D 121 . 3.961 −5.150 69.497 1.00 27.47 . 1 763 ATOM C CB LYS D 121 . 4.387 −2.116 70.285 1.00 26.71 . 1 764 ATOM C CG LYS D 121 . 4.080 −1.387 68.986 1.00 29.19 . 1 765 ATOM C CD LYS D 121 . 2.998 −0.330 69.233 1.00 31.66 . 1 766 ATOM C CE LYS D 121 . 2.578 0.378 67.953 1.00 30.16 . 1 767 ATOM N NZ LYS D 121 . 3.701 1.127 67.347 1.00 30.04 . 1 768 ATOM N N TYR D 122 . 5.323 −4.271 67.943 1.00 25.21 . 1 769 ATOM C CA TYR D 122 . 4.874 −5.213 66.922 1.00 26.77 . 1 770 ATOM C C TYR D 122 . 5.372 −6.646 67.173 1.00 27.58 . 1 771 ATOM O O TYR D 122 . 5.016 −7.578 66.442 1.00 28.28 . 1 772 ATOM C CB TYR D 122 . 5.306 −4.729 65.538 1.00 25.62 . 1 773 ATOM C CG TYR D 122 . 4.497 −3.546 65.050 1.00 24.70 . 1 774 ATOM C CD1 TYR D 122 . 5.000 −2.246 65.123 1.00 26.39 . 1 775 ATOM C CD2 TYR D 122 . 3.225 −3.732 64.505 1.00 27.40 . 1 776 ATOM C CE1 TYR D 122 . 4.250 −1.154 64.655 1.00 26.97 . 1 777 ATOM C CE2 TYR D 122 . 2.470 −2.655 64.036 1.00 27.81 . 1 778 ATOM C CZ TYR D 122 . 2.988 −1.374 64.114 1.00 27.54 . 1 779 ATOM O OH TYR D 122 . 2.235 −0.327 63.646 1.00 29.04 . 1 780 ATOM N N LEU D 123 . 6.187 −6.818 68.209 1.00 28.89 . 1 781 ATOM C CA LEU D 123 . 6.701 −8.138 68.553 1.00 30.32 . 1 782 ATOM C C LEU D 123 . 5.937 −8.707 69.743 1.00 31.37 . 1 783 ATOM O O LEU D 123 . 6.334 −9.716 70.317 1.00 31.53 . 1 784 ATOM C CB LEU D 123 . 8.191 −8.073 68.893 1.00 30.14 . 1 785 ATOM C CG LEU D 123 . 9.114 −7.375 67.897 1.00 33.17 . 1 786 ATOM C CD1 LEU D 123 . 10.554 −7.603 68.304 1.00 33.30 . 1 787 ATOM C CD2 LEU D 123 . 8.879 −7.906 66.502 1.00 30.99 . 1 788 ATOM N N VAL D 124 . 4.846 −8.046 70.114 1.00 32.47 . 1 789 ATOM C CA VAL D 124 . 4.008 −8.486 71.227 1.00 33.66 . 1 790 ATOM C C VAL D 124 . 2.760 −9.156 70.644 1.00 35.54 . 1 791 ATOM O O VAL D 124 . 1.998 −8.536 69.898 1.00 33.74 . 1 792 ATOM C CB VAL D 124 . 3.595 −7.287 72.110 1.00 33.42 . 1 793 ATOM C CG1 VAL D 124 . 2.771 −7.762 73.297 1.00 33.45 . 1 794 ATOM C CG2 VAL D 124 . 4.842 −6.543 72.576 1.00 32.34 . 1 795 ATOM N N PRO D 125 . 2.540 −10.439 70.975 1.00 35.73 . 1 796 ATOM C CA PRO D 125 . 1.397 −11.219 70.491 1.00 37.41 . 1 797 ATOM C C PRO D 125 . 0.032 −10.541 70.465 1.00 38.77 . 1 798 ATOM O O PRO D 125 . −0.701 −10.665 69.483 1.00 38.90 . 1 799 ATOM C CB PRO D 125 . 1.420 −12.447 71.397 1.00 38.44 . 1 800 ATOM C CG PRO D 125 . 2.888 −12.673 71.566 1.00 36.93 . 1 801 ATOM C CD PRO D 125 . 3.397 −11.266 71.848 1.00 37.07 . 1 802 ATOM N N ASP D 126 . −0.310 −9.818 71.524 1.00 39.23 . 1 803 ATOM C CA ASP D 126 . −1.616 −9.168 71.592 1.00 42.24 . 1 804 ATOM C C ASP D 126 . −1.690 −7.734 71.062 1.00 40.67 . 1 805 ATOM O O ASP D 126 . −2.731 −7.090 71.177 1.00 40.63 . 1 806 ATOM C CB ASP D 126 . −2.126 −9.191 73.035 1.00 46.65 . 1 807 ATOM C CG ASP D 126 . −1.190 −8.476 73.989 1.00 51.12 . 1 808 ATOM O OD1 ASP D 126 . −0.902 −7.281 73.757 1.00 53.75 . 1 809 ATOM O OD2 ASP D 126 . −0.741 −9.108 74.969 1.00 55.92 . 1 810 ATOM N N GLU D 127 . −0.595 −7.235 70.495 1.00 38.78 . 1 811 ATOM C CA GLU D 127 . −0.564 −5.876 69.954 1.00 36.76 . 1 812 ATOM C C GLU D 127 . −1.739 −5.645 69.002 1.00 36.86 . 1 813 ATOM O O GLU D 127 . −1.889 −6.352 68.006 1.00 34.77 . 1 814 ATOM C CB GLU D 127 . 0.763 −5.643 69.220 1.00 35.55 . 1 815 ATOM C CG GLU D 127 . 0.868 −4.326 68.448 1.00 34.54 . 1 816 ATOM C CD GLU D 127 . 0.473 −3.107 69.270 1.00 36.81 . 1 817 ATOM O OE1 GLU D 127 . 0.901 −3.003 70.441 1.00 34.73 . 1 818 ATOM O OE2 GLU D 127 . −0.263 −2.247 68.737 1.00 34.83 . 1 819 ATOM N N SER D 128 . −2.566 −4.649 69.304 1.00 36.61 . 1 820 ATOM C CA SER D 128 . −3.722 −4.363 68.466 1.00 38.29 . 1 821 ATOM C C SER D 128 . −3.351 −3.965 67.039 1.00 36.51 . 1 822 ATOM O O SER D 128 . −4.073 −4.298 66.100 1.00 37.41 . 1 823 ATOM C CB SER D 128 . −4.602 −3.286 69.120 1.00 40.28 . 1 824 ATOM O OG SER D 128 . −3.867 −2.117 69.417 1.00 42.77 . 1 825 ATOM N N ARG D 129 . −2.224 −3.269 66.875 1.00 36.02 . 1 826 ATOM C CA ARG D 129 . −1.751 −2.844 65.552 1.00 35.51 . 1 827 ATOM C C ARG D 129 . −1.342 −4.061 64.713 1.00 34.40 . 1 828 ATOM O O ARG D 129 . −1.216 −3.972 63.493 1.00 31.16 . 1 829 ATOM C CB ARG D 129 . −0.526 −1.930 65.678 1.00 37.50 . 1 830 ATOM C CG ARG D 129 . −0.751 −0.533 66.252 1.00 40.99 . 1 831 ATOM C CD ARG D 129 . −0.851 0.495 65.138 1.00 43.17 . 1 832 ATOM N NE ARG D 129 . −2.241 0.742 64.802 1.00 45.18 . 1 833 ATOM C CZ ARG D 129 . −2.668 1.220 63.644 1.00 44.29 . 1 834 ATOM N NH1 ARG D 129 . −1.813 1.511 62.673 1.00 46.49 . 1 835 ATOM N NH2 ARG D 129 . −3.966 1.412 63.466 1.00 46.35 . 1 836 ATOM N N GLY D 130 . −1.109 −5.188 65.377 1.00 32.27 . 1 837 ATOM C CA GLY D 130 . −0.700 −6.386 64.667 1.00 30.94 . 1 838 ATOM C C GLY D 130 . 0.560 −7.011 65.236 1.00 30.01 . 1 839 ATOM O O GLY D 130 . 1.369 −6.332 65.866 1.00 30.17 . 1 840 ATOM N N TYR D 131 . 0.722 −8.309 65.003 1.00 30.97 . 1 841 ATOM C CA TYR D 131 . 1.870 −9.071 65.486 1.00 28.20 . 1 842 ATOM C C TYR D 131 . 2.709 −9.531 64.295 1.00 28.20 . 1 843 ATOM O O TYR D 131 . 2.182 −10.126 63.358 1.00 29.69 . 1 844 ATOM C CB TYR D 131 . 1.361 −10.280 66.284 1.00 28.38 . 1 845 ATOM C CG TYR D 131 . 2.433 −11.147 66.904 1.00 30.96 . 1 846 ATOM C CD1 TYR D 131 . 3.438 −10.590 67.695 1.00 32.15 . 1 847 ATOM C CD2 TYR D 131 . 2.419 −12.538 66.740 1.00 30.55 . 1 848 ATOM C CE1 TYR D 131 . 4.399 −11.390 68.307 1.00 31.08 . 1 849 ATOM C CE2 TYR D 131 . 3.376 −13.346 67.349 1.00 30.90 . 1 850 ATOM C CZ TYR D 131 . 4.363 −12.764 68.131 1.00 31.67 . 1 851 ATOM O OH TYR D 131 . 5.327 −13.546 68.730 1.00 30.98 . 1 852 ATOM N N LEU D 132 . 4.013 −9.270 64.338 1.00 25.77 . 1 853 ATOM C CA LEU D 132 . 4.910 −9.632 63.245 1.00 25.99 . 1 854 ATOM C C LEU D 132 . 5.990 −10.659 63.585 1.00 26.29 . 1 855 ATOM O O LEU D 132 . 6.656 −11.174 62.684 1.00 27.24 . 1 856 ATOM C CB LEU D 132 . 5.599 −8.368 62.712 1.00 23.23 . 1 857 ATOM C CG LEU D 132 . 4.718 −7.299 62.061 1.00 23.16 . 1 858 ATOM C CD1 LEU D 132 . 5.558 −6.045 61.791 1.00 23.30 . 1 859 ATOM C CD2 LEU D 132 . 4.138 −7.846 60.751 1.00 21.04 . 1 860 ATOM N N ALA D 133 . 6.158 −10.966 64.871 1.00 26.35 . 1 861 ATOM C CA ALA D 133 . 7.204 −11.892 65.304 1.00 27.88 . 1 862 ATOM C C ALA D 133 . 7.034 −13.354 64.923 1.00 27.67 . 1 863 ATOM O O ALA D 133 . 8.023 −14.078 64.816 1.00 25.28 . 1 864 ATOM C CB ALA D 133 . 7.400 −11.787 66.825 1.00 27.33 . 1 865 ATOM N N SER D 134 . 5.799 −13.803 64.734 1.00 29.09 . 1 866 ATOM C CA SER D 134 . 5.592 −15.204 64.379 1.00 28.82 . 1 867 ATOM C C SER D 134 . 6.215 −15.549 63.034 1.00 28.30 . 1 868 ATOM O O SER D 134 . 6.480 −16.716 62.749 1.00 26.40 . 1 869 ATOM C CB SER D 134 . 4.100 −15.553 64.383 1.00 28.88 . 1 870 ATOM O OG SER D 134 . 3.370 −14.722 63.504 1.00 27.49 . 1 871 ATOM N N PHE D 135 . 6.462 −14.547 62.191 1.00 27.30 . 1 872 ATOM C CA PHE D 135 . 7.080 −14.858 60.917 1.00 26.00 . 1 873 ATOM C C PHE D 135 . 8.561 −15.139 61.109 1.00 23.87 . 1 874 ATOM O O PHE D 135 . 9.166 −15.868 60.330 1.00 25.34 . 1 875 ATOM C CB PHE D 135 . 6.910 −13.732 59.896 1.00 26.56 . 1 876 ATOM C CG PHE D 135 . 7.307 −14.144 58.507 1.00 27.50 . 1 877 ATOM C CD1 PHE D 135 . 6.472 −14.952 57.751 1.00 28.44 . 1 878 ATOM C CD2 PHE D 135 . 8.547 −13.793 57.989 1.00 28.69 . 1 879 ATOM C CE1 PHE D 135 . 6.869 −15.411 56.494 1.00 27.89 . 1 880 ATOM C CE2 PHE D 135 . 8.954 −14.248 56.734 1.00 28.34 . 1 881 ATOM C CZ PHE D 135 . 8.110 −15.060 55.989 1.00 28.21 . 1 882 ATOM N N THR D 136 . 9.154 −14.553 62.145 1.00 24.24 . 1 883 ATOM C CA THR D 136 . 10.563 −14.790 62.427 1.00 25.22 . 1 884 ATOM C C THR D 136 . 10.710 −16.270 62.794 1.00 26.78 . 1 885 ATOM O O THR D 136 . 11.667 −16.939 62.393 1.00 27.25 . 1 886 ATOM C CB THR D 136 . 11.058 −13.940 63.624 1.00 24.09 . 1 887 ATOM O OG1 THR D 136 . 10.950 −12.546 63.307 1.00 26.31 . 1 888 ATOM C CG2 THR D 136 . 12.507 −14.262 63.929 1.00 25.67 . 1 889 ATOM N N THR D 137 . 9.752 −16.758 63.575 1.00 27.65 . 1 890 ATOM C CA THR D 137 . 9.731 −18.155 64.008 1.00 28.10 . 1 891 ATOM C C THR D 137 . 9.713 −19.064 62.775 1.00 29.78 . 1 892 ATOM O O THR D 137 . 10.385 −20.096 62.734 1.00 30.01 . 1 893 ATOM C CB THR D 137 . 8.491 −18.418 64.880 1.00 29.32 . 1 894 ATOM O OG1 THR D 137 . 8.444 −17.446 65.938 1.00 28.14 . 1 895 ATOM C CG2 THR D 137 . 8.537 −19.829 65.478 1.00 26.88 . 1 896 ATOM N N PHE D 138 . 8.956 −18.668 61.757 1.00 31.45 . 1 897 ATOM C CA PHE D 138 . 8.894 −19.441 60.520 1.00 31.96 . 1 898 ATOM C C PHE D 138 . 10.256 −19.440 59.824 1.00 33.51 . 1 899 ATOM O O PHE D 138 . 10.785 −20.495 59.468 1.00 30.43 . 1 900 ATOM C CB PHE D 138 . 7.840 −18.855 59.575 1.00 34.14 . 1 901 ATOM C CG PHE D 138 . 7.916 −19.401 58.175 1.00 35.34 . 1 902 ATOM C CD1 PHE D 138 . 7.610 −20.734 57.915 1.00 35.76 . 1 903 ATOM C CD2 PHE D 138 . 8.330 −18.591 57.121 1.00 36.10 . 1 904 ATOM C CE1 PHE D 138 . 7.717 −21.255 56.628 1.00 35.81 . 1 905 ATOM C CE2 PHE D 138 . 8.442 −19.104 55.828 1.00 36.50 . 1 906 ATOM C CZ PHE D 138 . 8.134 −20.438 55.584 1.00 36.54 . 1 907 ATOM N N LEU D 139 . 10.827 −18.252 59.633 1.00 32.07 . 1 908 ATOM C CA LEU D 139 . 12.119 −18.142 58.968 1.00 32.77 . 1 909 ATOM C C LEU D 139 . 13.189 −18.974 59.663 1.00 32.97 . 1 910 ATOM O O LEU D 139 . 14.055 −19.563 59.013 1.00 32.35 . 1 911 ATOM C CB LEU D 139 . 12.563 −16.677 58.906 1.00 30.46 . 1 912 ATOM C CG LEU D 139 . 11.739 −15.785 57.970 1.00 30.46 . 1 913 ATOM C CD1 LEU D 139 . 12.248 −14.349 58.039 1.00 28.31 . 1 914 ATOM C CD2 LEU D 139 . 11.839 −16.310 56.534 1.00 30.40 . 1 915 ATOM N N CYS D 140 . 13.116 −19.025 60.987 1.00 35.39 . 1 916 ATOM C CA CYS D 140 . 14.083 −19.772 61.774 1.00 37.01 . 1 917 ATOM C C CYS D 140 . 13.755 −21.256 61.935 1.00 39.83 . 1 918 ATOM O O CYS D 140 . 14.442 −21.960 62.669 1.00 39.88 . 1 919 ATOM C CB CYS D 140 . 14.241 −19.125 63.153 1.00 36.77 . 1 920 ATOM S SG CYS D 140 . 14.997 −17.492 63.097 1.00 35.63 . 1 921 ATOM N N TYR D 141 . 12.716 −21.734 61.255 1.00 41.66 . 1 922 ATOM C CA TYR D 141 . 12.354 −23.148 61.350 1.00 44.32 . 1 923 ATOM C C TYR D 141 . 13.511 −23.995 60.809 1.00 45.27 . 1 924 ATOM O O TYR D 141 . 14.091 −23.673 59.776 1.00 45.44 . 1 925 ATOM C CB TYR D 141 . 11.084 −23.431 60.544 1.00 45.44 . 1 926 ATOM C CG TYR D 141 . 10.429 −24.754 60.881 1.00 48.11 . 1 927 ATOM C CD1 TYR D 141 . 9.789 −24.944 62.107 1.00 48.67 . 1 928 ATOM C CD2 TYR D 141 . 10.457 −25.820 59.980 1.00 48.29 . 1 929 ATOM C CE1 TYR D 141 . 9.190 −26.166 62.430 1.00 50.26 . 1 930 ATOM C CE2 TYR D 141 . 9.864 −27.046 60.290 1.00 50.08 . 1 931 ATOM C CZ TYR D 141 . 9.231 −27.213 61.516 1.00 51.01 . 1 932 ATOM O OH TYR D 141 . 8.633 −28.418 61.824 1.00 50.79 . 1 933 ATOM N N PRO D 142 . 13.856 −25.093 61.505 1.00 47.07 . 1 934 ATOM C CA PRO D 142 . 14.940 −26.015 61.137 1.00 47.53 . 1 935 ATOM C C PRO D 142 . 15.087 −26.332 59.646 1.00 48.25 . 1 936 ATOM O O PRO D 142 . 16.146 −26.120 59.059 1.00 49.20 . 1 937 ATOM C CB PRO D 142 . 14.620 −27.256 61.964 1.00 48.78 . 1 938 ATOM C CG PRO D 142 . 14.078 −26.657 63.223 1.00 48.67 . 1 939 ATOM C CD PRO D 142 . 13.143 −25.582 62.701 1.00 46.92 . 1 940 ATOM N N ALA D 143 . 14.029 −26.849 59.036 1.00 48.69 . 1 941 ATOM C CA ALA D 143 . 14.072 −27.187 57.618 1.00 49.69 . 1 942 ATOM C C ALA D 143 . 14.529 −26.004 56.761 1.00 50.46 . 1 943 ATOM O O ALA D 143 . 15.370 −26.152 55.871 1.00 51.09 . 1 944 ATOM C CB ALA D 143 . 12.698 −27.658 57.160 1.00 50.51 . 1 945 ATOM N N LEU D 144 . 13.981 −24.827 57.042 1.00 49.54 . 1 946 ATOM C CA LEU D 144 . 14.311 −23.631 56.282 1.00 49.50 . 1 947 ATOM C C LEU D 144 . 15.736 −23.129 56.488 1.00 49.45 . 1 948 ATOM O O LEU D 144 . 16.331 −22.563 55.577 1.00 48.21 . 1 949 ATOM C CB LEU D 144 . 13.306 −22.531 56.612 1.00 48.57 . 1 950 ATOM C CG LEU D 144 . 11.867 −22.987 56.353 1.00 49.61 . 1 951 ATOM C CD1 LEU D 144 . 10.900 −21.922 56.803 1.00 48.96 . 1 952 ATOM C CD2 LEU D 144 . 11.689 −23.297 54.873 1.00 49.15 . 1 953 ATOM N N LEU D 145 . 16.283 −23.340 57.680 1.00 50.78 . 1 954 ATOM C CA LEU D 145 . 17.643 −22.897 57.971 1.00 52.11 . 1 955 ATOM C C LEU D 145 . 18.623 −23.473 56.965 1.00 52.45 . 1 956 ATOM O O LEU D 145 . 19.468 −22.757 56.426 1.00 52.55 . 1 957 ATOM C CB LEU D 145 . 18.046 −23.317 59.383 1.00 52.56 . 1 958 ATOM C CG LEU D 145 . 17.347 −22.533 60.492 1.00 52.76 . 1 959 ATOM C CD1 LEU D 145 . 17.587 −23.215 61.828 1.00 54.21 . 1 960 ATOM C CD2 LEU D 145 . 17.857 −21.097 60.494 1.00 51.47 . 1 961 ATOM N N GLN D 146 . 18.508 −24.772 56.714 1.00 53.00 . 1 962 ATOM C CA GLN D 146 . 19.384 −25.424 55.758 1.00 53.17 . 1 963 ATOM C C GLN D 146 . 19.144 −24.854 54.367 1.00 51.05 . 1 964 ATOM O O GLN D 146 . 20.063 −24.771 53.552 1.00 51.03 . 1 965 ATOM C CB GLN D 146 . 19.145 −26.935 55.766 1.00 57.09 . 1 966 ATOM C CG GLN D 146 . 19.840 −27.644 56.913 1.00 61.63 . 1 967 ATOM C CD GLN D 146 . 21.355 −27.513 56.835 1.00 64.78 . 1 968 ATOM O OE1 GLN D 146 . 21.999 −28.105 55.963 1.00 65.42 . 1 969 ATOM N NE2 GLN D 146 . 21.928 −26.724 57.740 1.00 65.67 . 1 970 ATOM N N VAL D 147 . 17.907 −24.452 54.101 1.00 48.33 . 1 971 ATOM C CA VAL D 147 . 17.567 −23.882 52.806 1.00 46.18 . 1 972 ATOM C C VAL D 147 . 18.262 −22.535 52.655 1.00 45.27 . 1 973 ATOM O O VAL D 147 . 19.008 −22.309 51.700 1.00 43.30 . 1 974 ATOM C CB VAL D 147 . 16.045 −23.674 52.667 1.00 45.57 . 1 975 ATOM C CG1 VAL D 147 . 15.712 −23.141 51.288 1.00 46.34 . 1 976 ATOM C CG2 VAL D 147 . 15.323 −24.981 52.910 1.00 48.51 . 1 977 ATOM N N TRP D 148 . 18.024 −21.650 53.618 1.00 44.43 . 1 978 ATOM C CA TRP D 148 . 18.609 −20.316 53.588 1.00 44.25 . 1 979 ATOM C C TRP D 148 . 20.105 −20.348 53.303 1.00 43.55 . 1 980 ATOM O O TRP D 148 . 20.584 −19.671 52.392 1.00 43.58 . 1 981 ATOM C CB TRP D 148 . 18.358 −19.595 54.919 1.00 43.95 . 1 982 ATOM C CG TRP D 148 . 16.907 −19.461 55.301 1.00 44.13 . 1 983 ATOM C CD1 TRP D 148 . 16.402 −19.415 56.567 1.00 43.42 . 1 984 ATOM C CD2 TRP D 148 . 15.778 −19.381 54.419 1.00 45.84 . 1 985 ATOM N NE1 TRP D 148 . 15.033 −19.318 56.533 1.00 45.29 . 1 986 ATOM C CE2 TRP D 148 . 14.622 −19.295 55.228 1.00 46.32 . 1 987 ATOM C CE3 TRP D 148 . 15.630 −19.377 53.026 1.00 48.36 . 1 988 ATOM C CZ2 TRP D 148 . 13.333 −19.208 54.691 1.00 48.29 . 1 989 ATOM C CZ3 TRP D 148 . 14.345 −19.291 52.489 1.00 49.22 . 1 990 ATOM C CH2 TRP D 148 . 13.215 −19.208 53.323 1.00 49.52 . 1 991 ATOM N N MET D 149 . 20.837 −21.148 54.073 1.00 42.95 . 1 992 ATOM C CA MET D 149 . 22.285 −21.236 53.920 1.00 43.34 . 1 993 ATOM C C MET D 149 . 22.804 −21.959 52.678 1.00 42.34 . 1 994 ATOM O O MET D 149 . 24.013 −22.119 52.506 1.00 42.81 . 1 995 ATOM C CB MET D 149 . 22.893 −21.853 55.174 1.00 44.38 . 1 996 ATOM C CG MET D 149 . 22.740 −20.969 56.409 1.00 47.16 . 1 997 ATOM S SD MET D 149 . 23.327 −19.279 56.141 1.00 50.14 . 1 998 ATOM C CE MET D 149 . 21.874 −18.334 56.571 1.00 48.11 . 1 999 ATOM N N ASN D 150 . 21.892 −22.396 51.820 1.00 41.18 . 1 1000 ATOM C CA ASN D 150 . 22.260 −23.064 50.576 1.00 41.17 . 1 1001 ATOM C C ASN D 150 . 21.669 −22.227 49.450 1.00 39.73 . 1 1002 ATOM O O ASN D 150 . 21.461 −22.704 48.334 1.00 36.92 . 1 1003 ATOM C CB ASN D 150 . 21.693 −24.486 50.532 1.00 44.23 . 1 1004 ATOM C CG ASN D 150 . 22.473 −25.454 51.403 1.00 48.95 . 1 1005 ATOM O OD1 ASN D 150 . 23.684 −25.618 51.238 1.00 51.20 . 1 1006 ATOM N ND2 ASN D 150 . 21.783 −26.106 52.333 1.00 49.28 . 1 1007 ATOM N N PHE D 151 . 21.400 −20.966 49.775 1.00 38.11 . 1 1008 ATOM C CA PHE D 151 . 20.824 −20.000 48.846 1.00 38.53 . 1 1009 ATOM C C PHE D 151 . 21.476 −20.056 47.459 1.00 39.55 . 1 1010 ATOM O O PHE D 151 . 20.784 −20.055 46.439 1.00 39.51 . 1 1011 ATOM C CB PHE D 151 . 20.979 −18.593 49.429 1.00 37.37 . 1 1012 ATOM C CG PHE D 151 . 20.087 −17.564 48.797 1.00 36.26 . 1 1013 ATOM C CD1 PHE D 151 . 18.788 −17.375 49.254 1.00 33.15 . 1 1014 ATOM C CD2 PHE D 151 . 20.551 −16.776 47.746 1.00 35.85 . 1 1015 ATOM C CE1 PHE D 151 . 17.962 −16.414 48.676 1.00 32.26 . 1 1016 ATOM C CE2 PHE D 151 . 19.731 −15.814 47.161 1.00 36.16 . 1 1017 ATOM C CZ PHE D 151 . 18.433 −15.632 47.629 1.00 33.02 . 1 1018 ATOM N N LYS D 152 . 22.805 −20.104 47.436 1.00 40.01 . 1 1019 ATOM C CA LYS D 152 . 23.577 −20.145 46.191 1.00 42.65 . 1 1020 ATOM C C LYS D 152 . 23.103 −21.161 45.153 1.00 43.01 . 1 1021 ATOM O O LYS D 152 . 23.059 −20.857 43.964 1.00 43.18 . 1 1022 ATOM C CB LYS D 152 . 25.055 −20.422 46.492 1.00 42.55 . 1 1023 ATOM C CG LYS D 152 . 25.286 −21.703 47.282 1.00 45.52 . 1 1024 ATOM C CD LYS D 152 . 26.745 −22.150 47.256 1.00 47.82 . 1 1025 ATOM C CE LYS D 152 . 27.147 −22.648 45.871 1.00 52.14 . 1 1026 ATOM N NZ LYS D 152 . 28.536 −23.197 45.841 1.00 53.62 . 1 1027 ATOM N N GLU D 153 . 22.759 −22.364 45.601 1.00 44.76 . 1 1028 ATOM C CA GLU D 153 . 22.329 −23.421 44.689 1.00 47.60 . 1 1029 ATOM C C GLU D 153 . 21.123 −23.049 43.826 1.00 46.86 . 1 1030 ATOM O O GLU D 153 . 21.048 −23.434 42.656 1.00 46.55 . 1 1031 ATOM C CB GLU D 153 . 22.049 −24.712 45.473 1.00 50.65 . 1 1032 ATOM C CG GLU D 153 . 21.766 −25.929 44.585 1.00 57.19 . 1 1033 ATOM C CD GLU D 153 . 21.758 −27.247 45.354 1.00 60.13 . 1 1034 ATOM O OE1 GLU D 153 . 21.123 −27.310 46.430 1.00 61.62 . 1 1035 ATOM O OE2 GLU D 153 . 22.377 −28.226 44.875 1.00 62.04 . 1 1036 ATOM N N ALA D 154 . 20.189 −22.296 44.398 1.00 45.97 . 1 1037 ATOM C CA ALA D 154 . 18.996 −21.879 43.671 1.00 44.41 . 1 1038 ATOM C C ALA D 154 . 19.351 −20.796 42.664 1.00 44.11 . 1 1039 ATOM O O ALA D 154 . 18.631 −20.572 41.695 1.00 43.88 . 1 1040 ATOM C CB ALA D 154 . 17.945 −21.361 44.643 1.00 43.85 . 1 1041 ATOM N N VAL D 155 . 20.469 −20.124 42.902 1.00 42.98 . 1 1042 ATOM C CA VAL D 155 . 20.916 −19.069 42.012 1.00 43.64 . 1 1043 ATOM C C VAL D 155 . 21.563 −19.629 40.746 1.00 45.73 . 1 1044 ATOM O O VAL D 155 . 21.191 −19.259 39.633 1.00 46.58 . 1 1045 ATOM C CB VAL D 155 . 21.932 −18.144 42.725 1.00 42.54 . 1 1046 ATOM C CG1 VAL D 155 . 22.624 −17.236 41.718 1.00 40.94 . 1 1047 ATOM C CG2 VAL D 155 . 21.213 −17.300 43.770 1.00 41.76 . 1 1048 ATOM N N VAL D 156 . 22.517 −20.534 40.930 1.00 47.04 . 1 1049 ATOM C CA VAL D 156 . 23.260 −21.122 39.824 1.00 50.64 . 1 1050 ATOM C C VAL D 156 . 22.543 −22.199 39.010 1.00 53.21 . 1 1051 ATOM O O VAL D 156 . 22.764 −22.316 37.803 1.00 54.10 . 1 1052 ATOM C CB VAL D 156 . 24.595 −21.697 40.329 1.00 49.90 . 1 1053 ATOM C CG1 VAL D 156 . 25.410 −20.598 40.988 1.00 50.85 . 1 1054 ATOM C CG2 VAL D 156 . 24.335 −22.822 41.318 1.00 50.84 . 1 1055 ATOM N N ASP D 157 . 21.700 −22.990 39.662 1.00 55.56 . 1 1056 ATOM C CA ASP D 157 . 20.974 −24.046 38.964 1.00 57.47 . 1 1057 ATOM C C ASP D 157 . 19.604 −23.516 38.558 1.00 58.21 . 1 1058 ATOM O O ASP D 157 . 18.782 −23.204 39.416 1.00 58.74 . 1 1059 ATOM C CB ASP D 157 . 20.816 −25.268 39.875 1.00 58.38 . 1 1060 ATOM C CG ASP D 157 . 20.451 −26.528 39.106 1.00 60.00 . 1 1061 ATOM O OD1 ASP D 157 . 21.267 −26.971 38.268 1.00 61.29 . 1 1062 ATOM O OD2 ASP D 157 . 19.353 −27.074 39.335 1.00 59.79 . 1 1063 ATOM N N GLU D 158 . 19.355 −23.411 37.254 1.00 59.46 . 1 1064 ATOM C CA GLU D 158 . 18.074 −22.900 36.770 1.00 60.27 . 1 1065 ATOM C C GLU D 158 . 16.910 −23.674 37.384 1.00 60.83 . 1 1066 ATOM O O GLU D 158 . 15.745 −23.343 37.163 1.00 60.06 . 1 1067 ATOM C CB GLU D 158 . 18.011 −22.960 35.240 1.00 61.43 . 1 1068 ATOM C CG GLU D 158 . 16.779 −22.274 34.653 1.00 63.63 . 1 1069 ATOM C CD GLU D 158 . 16.892 −22.025 33.158 1.00 65.48 . 1 1070 ATOM O OE1 GLU D 158 . 17.173 −22.986 32.409 1.00 66.47 . 1 1071 ATOM O OE2 GLU D 158 . 16.694 −20.866 32.729 1.00 65.63 . 1 1072 ATOM N N ASP D 159 . 17.256 −24.703 38.157 1.00 62.00 . 1 1073 ATOM C CA ASP D 159 . 16.307 −25.554 38.873 1.00 63.07 . 1 1074 ATOM C C ASP D 159 . 14.924 −24.926 38.991 1.00 63.41 . 1 1075 ATOM O O ASP D 159 . 13.919 −25.631 39.060 1.00 64.33 . 1 1076 ATOM C CB ASP D 159 . 16.872 −25.857 40.271 1.00 63.86 . 1 1077 ATOM C CG ASP D 159 . 15.832 −26.414 41.231 1.00 64.83 . 1 1078 ATOM O OD1 ASP D 159 . 14.880 −25.683 41.582 1.00 64.75 . 1 1079 ATOM O OD2 ASP D 159 . 15.971 −27.585 41.646 1.00 65.75 . 1 1080 ATOM N N PHE D 174 . 5.588 −31.059 51.259 1.00 70.37 . 1 1081 ATOM C CA PHE D 174 . 6.182 −31.244 52.579 1.00 70.58 . 1 1082 ATOM C C PHE D 174 . 5.226 −30.764 53.671 1.00 71.33 . 1 1083 ATOM O O PHE D 174 . 5.576 −30.732 54.848 1.00 71.05 . 1 1084 ATOM C CB PHE D 174 . 7.509 −30.482 52.668 1.00 69.31 . 1 1085 ATOM C CG PHE D 174 . 8.327 −30.819 53.887 1.00 68.86 . 1 1086 ATOM C CD1 PHE D 174 . 8.764 −32.121 54.112 1.00 68.61 . 1 1087 ATOM C CD2 PHE D 174 . 8.667 −29.832 54.808 1.00 68.08 . 1 1088 ATOM C CE1 PHE D 174 . 9.531 −32.435 55.238 1.00 68.25 . 1 1089 ATOM C CE2 PHE D 174 . 9.431 −30.135 55.935 1.00 67.83 . 1 1090 ATOM C CZ PHE D 174 . 9.864 −31.440 56.150 1.00 67.69 . 1 1091 ATOM N N MET D 175 . 4.014 −30.391 53.273 1.00 72.82 . 1 1092 ATOM C CA MET D 175 . 3.004 −29.931 54.220 1.00 73.79 . 1 1093 ATOM C C MET D 175 . 2.652 −31.086 55.145 1.00 73.76 . 1 1094 ATOM O O MET D 175 . 3.007 −31.071 56.328 1.00 74.55 . 1 1095 ATOM C CB MET D 175 . 1.741 −29.467 53.483 1.00 76.08 . 1 1096 ATOM C CG MET D 175 . 0.691 −28.808 54.383 1.00 78.36 . 1 1097 ATOM S SD MET D 175 . 0.042 −29.857 55.717 1.00 81.92 . 1 1098 ATOM C CE MET D 175 . −1.427 −30.572 54.923 1.00 80.46 . 1 1099 ATOM N N GLY D 176 . 1.946 −32.078 54.600 1.00 72.29 . 1 1100 ATOM C CA GLY D 176 . 1.554 −33.237 55.381 1.00 70.28 . 1 1101 ATOM C C GLY D 176 . 2.731 −33.741 56.186 1.00 69.66 . 1 1102 ATOM O O GLY D 176 . 2.630 −33.952 57.397 1.00 68.92 . 1 1103 ATOM N N LYS D 177 . 3.856 −33.940 55.507 1.00 69.22 . 1 1104 ATOM C CA LYS D 177 . 5.064 −34.393 56.178 1.00 68.29 . 1 1105 ATOM C C LYS D 177 . 5.575 −33.202 56.972 1.00 67.49 . 1 1106 ATOM O O LYS D 177 . 6.354 −32.391 56.467 1.00 67.57 . 1 1107 ATOM C CB LYS D 177 . 6.112 −34.857 55.156 1.00 68.52 . 1 1108 ATOM C CG LYS D 177 . 7.515 −35.132 55.724 1.00 68.90 . 1 1109 ATOM C CD LYS D 177 . 7.497 −35.896 57.054 1.00 69.07 . 1 1110 ATOM C CE LYS D 177 . 7.605 −34.938 58.243 1.00 69.50 . 1 1111 ATOM N NZ LYS D 177 . 7.431 −35.610 59.560 1.00 68.52 . 1 1112 ATOM N N ASP D 178 . 5.102 −33.117 58.215 1.00 66.11 . 1 1113 ATOM C CA ASP D 178 . 5.438 −32.059 59.169 1.00 63.47 . 1 1114 ATOM C C ASP D 178 . 4.281 −31.073 59.301 1.00 62.00 . 1 1115 ATOM O O ASP D 178 . 4.269 −30.017 58.660 1.00 61.42 . 1 1116 ATOM C CB ASP D 178 . 6.699 −31.296 58.752 1.00 63.35 . 1 1117 ATOM C CG ASP D 178 . 7.298 −30.506 59.894 1.00 62.60 . 1 1118 ATOM O OD1 ASP D 178 . 6.522 −29.922 60.677 1.00 62.18 . 1 1119 ATOM O OD2 ASP D 178 . 8.541 −30.465 60.004 1.00 62.32 . 1 1120 ATOM N N LYS D 179 . 3.304 −31.427 60.130 1.00 59.80 . 1 1121 ATOM C CA LYS D 179 . 2.146 −30.573 60.352 1.00 57.92 . 1 1122 ATOM C C LYS D 179 . 2.567 −29.380 61.201 1.00 56.34 . 1 1123 ATOM O O LYS D 179 . 1.821 −28.410 61.347 1.00 54.80 . 1 1124 ATOM C CB LYS D 179 . 1.038 −31.352 61.070 1.00 58.59 . 1 1125 ATOM C CG LYS D 179 . 0.325 −32.394 60.210 1.00 59.83 . 1 1126 ATOM C CD LYS D 179 . −0.445 −31.738 59.073 1.00 61.26 . 1 1127 ATOM C CE LYS D 179 . −1.269 −32.753 58.287 1.00 63.06 . 1 1128 ATOM N NZ LYS D 179 . −2.370 −33.349 59.103 1.00 63.00 . 1 1129 ATOM N N LYS D 180 . 3.773 −29.467 61.752 1.00 54.25 . 1 1130 ATOM C CA LYS D 180 . 4.324 −28.421 62.598 1.00 53.52 . 1 1131 ATOM C C LYS D 180 . 4.708 −27.189 61.787 1.00 51.83 . 1 1132 ATOM O O LYS D 180 . 4.262 −26.079 62.071 1.00 52.00 . 1 1133 ATOM C CB LYS D 180 . 5.554 −28.952 63.329 1.00 55.31 . 1 1134 ATOM C CG LYS D 180 . 6.185 −27.963 64.282 1.00 57.90 . 1 1135 ATOM C CD LYS D 180 . 7.485 −28.505 64.847 1.00 61.29 . 1 1136 ATOM C CE LYS D 180 . 8.070 −27.563 65.880 1.00 62.00 . 1 1137 ATOM N NZ LYS D 180 . 9.431 −27.982 66.291 1.00 63.83 . 1 1138 ATOM N N MET D 181 . 5.545 −27.396 60.780 1.00 49.95 . 1 1139 ATOM C CA MET D 181 . 5.992 −26.307 59.928 1.00 48.73 . 1 1140 ATOM C C MET D 181 . 4.808 −25.619 59.268 1.00 47.82 . 1 1141 ATOM O O MET D 181 . 4.758 −24.392 59.181 1.00 47.37 . 1 1142 ATOM C CB MET D 181 . 6.927 −26.839 58.851 1.00 49.45 . 1 1143 ATOM C CG MET D 181 . 7.465 −25.769 57.939 1.00 49.25 . 1 1144 ATOM S SD MET D 181 . 8.525 −26.450 56.686 1.00 51.31 . 1 1145 ATOM C CE MET D 181 . 8.416 −25.164 55.441 1.00 50.66 . 1 1146 ATOM N N ASN D 182 . 3.856 −26.417 58.796 1.00 46.03 . 1 1147 ATOM C CA ASN D 182 . 2.677 −25.876 58.143 1.00 45.00 . 1 1148 ATOM C C ASN D 182 . 1.933 −24.968 59.120 1.00 43.24 . 1 1149 ATOM O O ASN D 182 . 1.484 −23.881 58.756 1.00 39.77 . 1 1150 ATOM C CB ASN D 182 . 1.770 −27.020 57.671 1.00 47.74 . 1 1151 ATOM C CG ASN D 182 . 0.539 −26.527 56.931 1.00 50.05 . 1 1152 ATOM O OD1 ASN D 182 . −0.569 −26.544 57.468 1.00 51.62 . 1 1153 ATOM N ND2 ASN D 182 . 0.729 −26.080 55.694 1.00 50.19 . 1 1154 ATOM N N GLN D 183 . 1.826 −25.419 60.365 1.00 40.69 . 1 1155 ATOM C CA GLN D 183 . 1.140 −24.668 61.408 1.00 40.96 . 1 1156 ATOM C C GLN D 183 . 1.842 −23.335 61.681 1.00 39.29 . 1 1157 ATOM O O GLN D 183 . 1.196 −22.295 61.806 1.00 36.41 . 1 1158 ATOM C CB GLN D 183 . 1.089 −25.507 62.690 1.00 43.43 . 1 1159 ATOM C CG GLN D 183 . 0.200 −24.954 63.795 1.00 46.05 . 1 1160 ATOM C CD GLN D 183 . 0.830 −23.796 64.550 1.00 49.97 . 1 1161 ATOM O OE1 GLN D 183 . 1.926 −23.917 65.100 1.00 51.38 . 1 1162 ATOM N NE2 GLN D 183 . 0.132 −22.667 64.587 1.00 52.39 . 1 1163 ATOM N N ILE D 184 . 3.166 −23.381 61.779 1.00 37.58 . 1 1164 ATOM C CA ILE D 184 . 3.952 −22.186 62.035 1.00 38.58 . 1 1165 ATOM C C ILE D 184 . 3.859 −21.234 60.845 1.00 38.73 . 1 1166 ATOM O O ILE D 184 . 3.696 −20.031 61.021 1.00 35.72 . 1 1167 ATOM C CB ILE D 184 . 5.426 −22.545 62.284 1.00 39.70 . 1 1168 ATOM C CG1 ILE D 184 . 5.559 −23.250 63.635 1.00 41.14 . 1 1169 ATOM C CG2 ILE D 184 . 6.292 −21.293 62.234 1.00 39.29 . 1 1170 ATOM C CD1 ILE D 184 . 6.955 −23.783 63.914 1.00 43.63 . 1 1171 ATOM N N PHE D 185 . 3.956 −21.783 59.637 1.00 38.01 . 1 1172 ATOM C CA PHE D 185 . 3.873 −20.973 58.430 1.00 38.45 . 1 1173 ATOM C C PHE D 185 . 2.519 −20.291 58.323 1.00 38.20 . 1 1174 ATOM O O PHE D 185 . 2.444 −19.078 58.125 1.00 37.35 . 1 1175 ATOM C CB PHE D 185 . 4.094 −21.826 57.179 1.00 39.32 . 1 1176 ATOM C CG PHE D 185 . 3.796 −21.095 55.901 1.00 40.74 . 1 1177 ATOM C CD1 PHE D 185 . 4.584 −20.021 55.503 1.00 40.25 . 1 1178 ATOM C CD2 PHE D 185 . 2.702 −21.451 55.119 1.00 41.59 . 1 1179 ATOM C CE1 PHE D 185 . 4.289 −19.308 54.347 1.00 41.01 . 1 1180 ATOM C CE2 PHE D 185 . 2.396 −20.744 53.958 1.00 41.81 . 1 1181 ATOM C CZ PHE D 185 . 3.192 −19.669 53.573 1.00 41.24 . 1 1182 ATOM N N ASN D 186 . 1.451 −21.072 58.458 1.00 37.53 . 1 1183 ATOM C CA ASN D 186 . 0.104 −20.528 58.357 1.00 38.08 . 1 1184 ATOM C C ASN D 186 . −0.181 −19.484 59.415 1.00 37.62 . 1 1185 ATOM O O ASN D 186 . −0.809 −18.462 59.134 1.00 36.27 . 1 1186 ATOM C CB ASN D 186 . −0.944 −21.634 58.461 1.00 40.85 . 1 1187 ATOM C CG ASN D 186 . −0.873 −22.606 57.309 1.00 44.35 . 1 1188 ATOM O OD1 ASN D 186 . −0.795 −22.204 56.150 1.00 45.34 . 1 1189 ATOM N ND2 ASN D 186 . −0.905 −23.898 57.619 1.00 47.03 . 1 1190 ATOM N N LYS D 187 . 0.268 −19.742 60.637 1.00 35.44 . 1 1191 ATOM C CA LYS D 187 . 0.035 −18.796 61.711 1.00 35.60 . 1 1192 ATOM C C LYS D 187 . 0.689 −17.449 61.397 1.00 33.83 . 1 1193 ATOM O O LYS D 187 . 0.081 −16.399 61.596 1.00 30.87 . 1 1194 ATOM C CB LYS D 187 . 0.575 −19.353 63.030 1.00 38.82 . 1 1195 ATOM C CG LYS D 187 . 0.368 −18.435 64.217 1.00 42.26 . 1 1196 ATOM C CD LYS D 187 . 0.184 −19.235 65.499 1.00 48.17 . 1 1197 ATOM C CE LYS D 187 . −1.084 −20.096 65.438 1.00 50.11 . 1 1198 ATOM N NZ LYS D 187 . −1.283 −20.910 66.676 1.00 51.55 . 1 1199 ATOM N N SER D 188 . 1.921 −17.485 60.901 1.00 33.28 . 1 1200 ATOM C CA SER D 188 . 2.638 −16.253 60.587 1.00 33.75 . 1 1201 ATOM C C SER D 188 . 1.962 −15.477 59.456 1.00 32.98 . 1 1202 ATOM O O SER D 188 . 1.987 −14.244 59.430 1.00 30.69 . 1 1203 ATOM C CB SER D 188 . 4.104 −16.557 60.229 1.00 33.09 . 1 1204 ATOM O OG SER D 188 . 4.237 −17.187 58.970 1.00 32.92 . 1 1205 ATOM N N MET D 189 . 1.349 −16.194 58.521 1.00 31.27 . 1 1206 ATOM C CA MET D 189 . 0.673 −15.526 57.416 1.00 32.85 . 1 1207 ATOM C C MET D 189 . −0.552 −14.795 57.946 1.00 31.98 . 1 1208 ATOM O O MET D 189 . −0.854 −13.671 57.539 1.00 31.18 . 1 1209 ATOM C CB MET D 189 . 0.263 −16.550 56.363 1.00 34.00 . 1 1210 ATOM C CG MET D 189 . 1.437 −17.257 55.743 1.00 39.38 . 1 1211 ATOM S SD MET D 189 . 2.369 −16.149 54.692 1.00 46.17 . 1 1212 ATOM C CE MET D 189 . 1.535 −16.469 53.129 1.00 48.19 . 1 1213 ATOM N N VAL D 190 . −1.254 −15.443 58.866 1.00 30.75 . 1 1214 ATOM C CA VAL D 190 . −2.439 −14.864 59.466 1.00 30.43 . 1 1215 ATOM C C VAL D 190 . −2.100 −13.561 60.183 1.00 29.44 . 1 1216 ATOM O O VAL D 190 . −2.798 −12.554 60.024 1.00 28.45 . 1 1217 ATOM C CB VAL D 190 . −3.074 −15.841 60.493 1.00 31.92 . 1 1218 ATOM C CG1 VAL D 190 . −4.132 −15.119 61.312 1.00 32.55 . 1 1219 ATOM C CG2 VAL D 190 . −3.693 −17.040 59.764 1.00 33.80 . 1 1220 ATOM N N ASP D 191 . −1.030 −13.592 60.971 1.00 26.90 . 1 1221 ATOM C CA ASP D 191 . −0.601 −12.430 61.749 1.00 27.20 . 1 1222 ATOM C C ASP D 191 . −0.090 −11.269 60.879 1.00 27.19 . 1 1223 ATOM O O ASP D 191 . −0.478 −10.114 61.082 1.00 27.44 . 1 1224 ATOM C CB ASP D 191 . 0.493 −12.838 62.748 1.00 27.54 . 1 1225 ATOM C CG ASP D 191 . 0.034 −13.924 63.725 1.00 29.73 . 1 1226 ATOM O OD1 ASP D 191 . −1.180 −14.036 63.984 1.00 29.23 . 1 1227 ATOM O OD2 ASP D 191 . 0.899 −14.657 64.252 1.00 31.69 . 1 1228 ATOM N N VAL D 192 . 0.783 −11.575 59.927 1.00 25.42 . 1 1229 ATOM C CA VAL D 192 . 1.326 −10.551 59.037 1.00 26.54 . 1 1230 ATOM C C VAL D 192 . 0.183 −9.946 58.231 1.00 28.85 . 1 1231 ATOM O O VAL D 192 . 0.073 −8.725 58.090 1.00 28.66 . 1 1232 ATOM C CB VAL D 192 . 2.385 −11.154 58.078 1.00 25.53 . 1 1233 ATOM C CG1 VAL D 192 . 2.851 −10.113 57.059 1.00 22.30 . 1 1234 ATOM C CG2 VAL D 192 . 3.579 −11.644 58.881 1.00 28.08 . 1 1235 ATOM N N CYS D 193 . −0.688 −10.812 57.723 1.00 28.02 . 1 1236 ATOM C CA CYS D 193 . −1.819 −10.359 56.931 1.00 29.51 . 1 1237 ATOM C C CYS D 193 . −2.747 −9.429 57.713 1.00 28.56 . 1 1238 ATOM O O CYS D 193 . −3.199 −8.402 57.190 1.00 29.15 . 1 1239 ATOM C CB CYS D 193 . −2.598 −11.559 56.415 1.00 29.55 . 1 1240 ATOM S SG CYS D 193 . −3.694 −11.129 55.079 1.00 37.63 . 1 1241 ATOM N N ALA D 194 . −3.042 −9.785 58.959 1.00 25.50 . 1 1242 ATOM C CA ALA D 194 . −3.914 −8.956 59.787 1.00 27.83 . 1 1243 ATOM C C ALA D 194 . −3.257 −7.598 60.013 1.00 27.00 . 1 1244 ATOM O O ALA D 194 . −3.940 −6.571 60.082 1.00 25.59 . 1 1245 ATOM C CB ALA D 194 . −4.193 −9.634 61.133 1.00 25.41 . 1 1246 ATOM N N THR D 195 . −1.932 −7.605 60.141 1.00 26.73 . 1 1247 ATOM C CA THR D 195 . −1.180 −6.370 60.351 1.00 27.92 . 1 1248 ATOM C C THR D 195 . −1.283 −5.474 59.111 1.00 27.71 . 1 1249 ATOM O O THR D 195 . −1.500 −4.262 59.221 1.00 27.97 . 1 1250 ATOM C CB THR D 195 . 0.316 −6.667 60.647 1.00 28.02 . 1 1251 ATOM O OG1 THR D 195 . 0.423 −7.471 61.835 1.00 27.00 . 1 1252 ATOM C CG2 THR D 195 . 1.085 −5.370 60.866 1.00 26.26 . 1 1253 ATOM N N GLU D 196 . −1.136 −6.076 57.936 1.00 26.23 . 1 1254 ATOM C CA GLU D 196 . −1.211 −5.330 56.681 1.00 28.27 . 1 1255 ATOM C C GLU D 196 . −2.610 −4.810 56.421 1.00 27.56 . 1 1256 ATOM O O GLU D 196 . −2.783 −3.671 55.995 1.00 29.56 . 1 1257 ATOM C CB GLU D 196 . −0.803 −6.213 55.495 1.00 26.82 . 1 1258 ATOM C CG GLU D 196 . 0.603 −6.766 55.573 1.00 29.32 . 1 1259 ATOM C CD GLU D 196 . 0.871 −7.791 54.493 1.00 28.46 . 1 1260 ATOM O OE1 GLU D 196 . −0.008 −8.645 54.261 1.00 32.32 . 1 1261 ATOM O OE2 GLU D 196 . 1.958 −7.757 53.889 1.00 31.06 . 1 1262 ATOM N N MET D 197 . −3.612 −5.647 56.670 1.00 28.05 . 1 1263 ATOM C CA MET D 197 . −4.994 −5.262 56.426 1.00 29.69 . 1 1264 ATOM C C MET D 197 . −5.487 −4.153 57.344 1.00 29.95 . 1 1265 ATOM O O MET D 197 . −6.283 −3.313 56.919 1.00 32.15 . 1 1266 ATOM C CB MET D 197 . −5.923 −6.473 56.551 1.00 30.48 . 1 1267 ATOM C CG MET D 197 . −5.766 −7.509 55.450 1.00 31.39 . 1 1268 ATOM S SD MET D 197 . −6.073 −6.847 53.793 1.00 33.24 . 1 1269 ATOM C CE MET D 197 . −7.792 −6.549 53.860 1.00 31.72 . 1 1270 ATOM N N LYS D 198 . −5.028 −4.142 58.594 1.00 28.79 . 1 1271 ATOM C CA LYS D 198 . −5.470 −3.106 59.522 1.00 30.25 . 1 1272 ATOM C C LYS D 198 . −5.049 −1.728 59.021 1.00 29.83 . 1 1273 ATOM O O LYS D 198 . −5.863 −0.803 58.963 1.00 31.40 . 1 1274 ATOM C CB LYS D 198 . −4.899 −3.325 60.925 1.00 29.54 . 1 1275 ATOM C CG LYS D 198 . −5.448 −2.325 61.945 1.00 32.22 . 1 1276 ATOM C CD LYS D 198 . −4.871 −2.521 63.338 1.00 33.19 . 1 1277 ATOM C CE LYS D 198 . −5.330 −1.412 64.297 1.00 32.91 . 1 1278 ATOM N NZ LYS D 198 . −6.809 −1.361 64.492 1.00 30.68 . 1 1279 ATOM N N ARG D 199 . −3.777 −1.595 58.665 1.00 29.36 . 1 1280 ATOM C CA ARG D 199 . −3.262 −0.323 58.176 1.00 31.81 . 1 1281 ATOM C C ARG D 199 . −3.858 0.030 56.815 1.00 33.13 . 1 1282 ATOM O O ARG D 199 . −4.257 1.169 56.580 1.00 32.12 . 1 1283 ATOM C CB ARG D 199 . −1.736 −0.374 58.083 1.00 32.03 . 1 1284 ATOM C CG ARG D 199 . −1.098 0.786 57.327 1.00 35.35 . 1 1285 ATOM C CD ARG D 199 . −0.783 1.996 58.193 1.00 39.01 . 1 1286 ATOM N NE ARG D 199 . −1.963 2.709 58.657 1.00 39.57 . 1 1287 ATOM C CZ ARG D 199 . −2.038 4.035 58.766 1.00 37.85 . 1 1288 ATOM N NH1 ARG D 199 . −1.005 4.791 58.435 1.00 39.68 . 1 1289 ATOM N NH2 ARG D 199 . −3.144 4.603 59.217 1.00 33.27 . 1 1290 ATOM N N MET D 200 . −3.930 −0.953 55.924 1.00 32.78 . 1 1291 ATOM C CA MET D 200 . −4.482 −0.721 54.601 1.00 34.62 . 1 1292 ATOM C C MET D 200 . −5.901 −0.157 54.680 1.00 35.57 . 1 1293 ATOM O O MET D 200 . −6.246 0.783 53.962 1.00 36.46 . 1 1294 ATOM C CB MET D 200 . −4.467 −2.024 53.798 1.00 35.00 . 1 1295 ATOM C CG MET D 200 . −4.867 −1.857 52.346 1.00 39.80 . 1 1296 ATOM S SD MET D 200 . −6.626 −2.130 52.086 1.00 44.40 . 1 1297 ATOM C CE MET D 200 . −6.543 −3.684 51.243 1.00 42.06 . 1 1298 ATOM N N LEU D 201 . −6.721 −0.714 55.564 1.00 35.04 . 1 1299 ATOM C CA LEU D 201 . −8.090 −0.245 55.701 1.00 35.31 . 1 1300 ATOM C C LEU D 201 . −8.216 1.161 56.291 1.00 36.29 . 1 1301 ATOM O O LEU D 201 . −9.233 1.828 56.099 1.00 36.70 . 1 1302 ATOM C CB LEU D 201 . −8.903 −1.251 56.521 1.00 34.89 . 1 1303 ATOM C CG LEU D 201 . −9.247 −2.497 55.692 1.00 34.95 . 1 1304 ATOM C CD1 LEU D 201 . −9.851 −3.586 56.563 1.00 36.34 . 1 1305 ATOM C CD2 LEU D 201 . −10.218 −2.094 54.592 1.00 35.44 . 1 1306 ATOM N N GLU D 202 . −7.185 1.618 56.993 1.00 36.11 . 1 1307 ATOM C CA GLU D 202 . −7.218 2.952 57.583 1.00 36.63 . 1 1308 ATOM C C GLU D 202 . −6.867 4.030 56.561 1.00 36.54 . 1 1309 ATOM O O GLU D 202 . −7.264 5.181 56.716 1.00 36.98 . 1 1310 ATOM C CB GLU D 202 . −6.226 3.063 58.747 1.00 36.54 . 1 1311 ATOM C CG GLU D 202 . −6.398 2.030 59.845 1.00 37.09 . 1 1312 ATOM C CD GLU D 202 . −5.382 2.197 60.961 1.00 36.74 . 1 1313 ATOM O OE1 GLU D 202 . −4.187 2.396 60.659 1.00 36.19 . 1 1314 ATOM O OE2 GLU D 202 . −5.780 2.120 62.142 1.00 37.87 . 1 1315 ATOM N N ILE D 203 . −6.137 3.656 55.514 1.00 36.47 . 1 1316 ATOM C CA ILE D 203 . −5.702 4.630 54.518 1.00 36.23 . 1 1317 ATOM C C ILE D 203 . −6.319 4.551 53.128 1.00 37.57 . 1 1318 ATOM O O ILE D 203 . −6.403 5.563 52.435 1.00 37.91 . 1 1319 ATOM C CB ILE D 203 . −4.173 4.576 54.357 1.00 36.47 . 1 1320 ATOM C CG1 ILE D 203 . −3.757 3.226 53.764 1.00 35.31 . 1 1321 ATOM C CG2 ILE D 203 . −3.509 4.775 55.715 1.00 36.37 . 1 1322 ATOM C CD1 ILE D 203 . −2.278 3.110 53.471 1.00 34.71 . 1 1323 ATOM N N TYR D 204 . −6.740 3.364 52.707 1.00 36.77 . 1 1324 ATOM C CA TYR D 204 . −7.323 3.216 51.381 1.00 37.69 . 1 1325 ATOM C C TYR D 204 . −8.814 3.507 51.382 1.00 39.48 . 1 1326 ATOM O O TYR D 204 . −9.580 2.909 52.136 1.00 38.97 . 1 1327 ATOM C CB TYR D 204 . −7.066 1.808 50.850 1.00 35.69 . 1 1328 ATOM C CG TYR D 204 . −7.641 1.541 49.480 1.00 34.96 . 1 1329 ATOM C CD1 TYR D 204 . −7.284 2.324 48.379 1.00 31.07 . 1 1330 ATOM C CD2 TYR D 204 . −8.488 0.454 49.270 1.00 33.66 . 1 1331 ATOM C CE1 TYR D 204 . −7.753 2.017 47.102 1.00 32.00 . 1 1332 ATOM C CE2 TYR D 204 . −8.962 0.143 48.001 1.00 33.16 . 1 1333 ATOM C CZ TYR D 204 . −8.589 0.922 46.924 1.00 32.36 . 1 1334 ATOM O OH TYR D 204 . −9.035 0.577 45.670 1.00 35.22 . 1 1335 ATOM N N THR D 205 . −9.216 4.433 50.522 1.00 41.51 . 1 1336 ATOM C CA THR D 205 . −10.610 4.834 50.416 1.00 44.58 . 1 1337 ATOM C C THR D 205 . −11.243 4.384 49.104 1.00 44.77 . 1 1338 ATOM O O THR D 205 . −12.331 4.837 48.744 1.00 46.99 . 1 1339 ATOM C CB THR D 205 . −10.735 6.365 50.530 1.00 45.40 . 1 1340 ATOM O OG1 THR D 205 . −9.813 6.988 49.627 1.00 47.41 . 1 1341 ATOM C CG2 THR D 205 . −10.423 6.818 51.945 1.00 48.85 . 1 1342 ATOM N N GLY D 206 . −10.569 3.482 48.398 1.00 43.86 . 1 1343 ATOM C CA GLY D 206 . −11.086 3.003 47.128 1.00 41.77 . 1 1344 ATOM C C GLY D 206 . −12.159 1.926 47.188 1.00 41.97 . 1 1345 ATOM O O GLY D 206 . −12.636 1.474 46.146 1.00 40.99 . 1 1346 ATOM N N PHE D 207 . −12.542 1.503 48.389 1.00 43.06 . 1 1347 ATOM C CA PHE D 207 . −13.573 0.475 48.527 1.00 42.81 . 1 1348 ATOM C C PHE D 207 . −14.975 1.070 48.450 1.00 45.04 . 1 1349 ATOM O O PHE D 207 . −15.936 0.376 48.111 1.00 45.20 . 1 1350 ATOM C CB PHE D 207 . −13.406 −0.277 49.850 1.00 40.19 . 1 1351 ATOM C CG PHE D 207 . −12.280 −1.271 49.846 1.00 37.70 . 1 1352 ATOM C CD1 PHE D 207 . −11.310 −1.248 50.843 1.00 37.59 . 1 1353 ATOM C CD2 PHE D 207 . −12.189 −2.235 48.844 1.00 36.47 . 1 1354 ATOM C CE1 PHE D 207 . −10.260 −2.167 50.844 1.00 37.71 . 1 1355 ATOM C CE2 PHE D 207 . −11.145 −3.161 48.835 1.00 36.30 . 1 1356 ATOM C CZ PHE D 207 . −10.178 −3.126 49.837 1.00 37.43 . 1 1357 ATOM N N GLU D 208 . −15.087 2.356 48.764 1.00 47.03 . 1 1358 ATOM C CA GLU D 208 . −16.374 3.048 48.737 1.00 50.47 . 1 1359 ATOM C C GLU D 208 . −16.963 3.018 47.326 1.00 49.65 . 1 1360 ATOM O O GLU D 208 . −16.289 3.377 46.362 1.00 51.25 . 1 1361 ATOM C CB GLU D 208 . −16.194 4.506 49.183 1.00 52.97 . 1 1362 ATOM C CG GLU D 208 . −17.464 5.175 49.680 1.00 57.30 . 1 1363 ATOM C CD GLU D 208 . −17.796 4.804 51.116 1.00 60.70 . 1 1364 ATOM O OE1 GLU D 208 . −18.928 5.089 51.565 1.00 62.66 . 1 1365 ATOM O OE2 GLU D 208 . −16.919 4.236 51.803 1.00 63.35 . 1 1366 ATOM N N GLY D 209 . −18.213 2.577 47.206 1.00 50.00 . 1 1367 ATOM C CA GLY D 209 . −18.855 2.533 45.902 1.00 48.50 . 1 1368 ATOM C C GLY D 209 . −18.915 1.178 45.215 1.00 48.66 . 1 1369 ATOM O O GLY D 209 . −19.602 1.026 44.201 1.00 46.76 . 1 1370 ATOM N N ILE D 210 . −18.203 0.193 45.756 1.00 46.82 . 1 1371 ATOM C CA ILE D 210 . −18.191 −1.145 45.172 1.00 45.17 . 1 1372 ATOM C C ILE D 210 . −19.440 −1.930 45.571 1.00 44.76 . 1 1373 ATOM O O ILE D 210 . −19.821 −1.944 46.742 1.00 44.67 . 1 1374 ATOM C CB ILE D 210 . −16.951 −1.949 45.640 1.00 45.73 . 1 1375 ATOM C CG1 ILE D 210 . −15.676 −1.140 45.397 1.00 46.39 . 1 1376 ATOM C CG2 ILE D 210 . −16.882 −3.278 44.906 1.00 42.38 . 1 1377 ATOM C CD1 ILE D 210 . −15.454 −0.765 43.960 1.00 48.41 . 1 1378 ATOM N N SER D 211 . −20.080 −2.580 44.603 1.00 43.39 . 1 1379 ATOM C CA SER D 211 . −21.268 −3.374 44.897 1.00 43.61 . 1 1380 ATOM C C SER D 211 . −20.878 −4.834 45.111 1.00 42.09 . 1 1381 ATOM O O SER D 211 . −21.320 −5.467 46.070 1.00 41.67 . 1 1382 ATOM C CB SER D 211 . −22.299 −3.249 43.766 1.00 44.07 . 1 1383 ATOM O OG SER D 211 . −21.684 −3.317 42.494 1.00 48.68 . 1 1384 ATOM N N THR D 212 . −20.050 −5.360 44.214 1.00 40.54 . 1 1385 ATOM C CA THR D 212 . −19.576 −6.736 44.316 1.00 40.69 . 1 1386 ATOM C C THR D 212 . −18.054 −6.761 44.219 1.00 39.70 . 1 1387 ATOM O O THR D 212 . −17.479 −6.355 43.209 1.00 40.98 . 1 1388 ATOM C CB THR D 212 . −20.162 −7.634 43.200 1.00 40.68 . 1 1389 ATOM O OG1 THR D 212 . −21.574 −7.785 43.397 1.00 41.26 . 1 1390 ATOM C CG2 THR D 212 . −19.508 −9.012 43.227 1.00 38.42 . 1 1391 ATOM N N LEU D 213 . −17.404 −7.221 45.281 1.00 37.95 . 1 1392 ATOM C CA LEU D 213 . −15.950 −7.299 45.307 1.00 35.96 . 1 1393 ATOM C C LEU D 213 . −15.512 −8.758 45.280 1.00 35.46 . 1 1394 ATOM O O LEU D 213 . −15.917 −9.551 46.127 1.00 35.07 . 1 1395 ATOM C CB LEU D 213 . −15.401 −6.627 46.568 1.00 36.15 . 1 1396 ATOM C CG LEU D 213 . −13.888 −6.749 46.767 1.00 35.56 . 1 1397 ATOM C CD1 LEU D 213 . −13.157 −6.056 45.620 1.00 36.67 . 1 1398 ATOM C CD2 LEU D 213 . −13.499 −6.143 48.107 1.00 34.49 . 1 1399 ATOM N N VAL D 214 . −14.685 −9.105 44.305 1.00 33.45 . 1 1400 ATOM C CA VAL D 214 . −14.205 −10.472 44.178 1.00 33.34 . 1 1401 ATOM C C VAL D 214 . −12.751 −10.556 44.635 1.00 32.62 . 1 1402 ATOM O O VAL D 214 . −11.882 −9.873 44.097 1.00 32.34 . 1 1403 ATOM C CB VAL D 214 . −14.272 −10.968 42.713 1.00 33.05 . 1 1404 ATOM C CG1 VAL D 214 . −13.865 −12.430 42.651 1.00 32.89 . 1 1405 ATOM C CG2 VAL D 214 . −15.678 −10.777 42.143 1.00 33.58 . 1 1406 ATOM N N ASP D 215 . −12.488 −11.388 45.634 1.00 30.07 . 1 1407 ATOM C CA ASP D 215 . −11.121 −11.542 46.102 1.00 29.21 . 1 1408 ATOM C C ASP D 215 . −10.535 −12.732 45.361 1.00 27.43 . 1 1409 ATOM O O ASP D 215 . −10.783 −13.880 45.728 1.00 27.78 . 1 1410 ATOM C CB ASP D 215 . −11.080 −11.806 47.606 1.00 27.86 . 1 1411 ATOM C CG ASP D 215 . −9.685 −11.664 48.171 1.00 29.69 . 1 1412 ATOM O OD1 ASP D 215 . −8.717 −11.822 47.394 1.00 30.74 . 1 1413 ATOM O OD2 ASP D 215 . −9.556 −11.404 49.386 1.00 31.60 . 1 1414 ATOM N N VAL D 216 . −9.767 −12.437 44.316 1.00 26.17 . 1 1415 ATOM C CA VAL D 216 . −9.135 −13.445 43.468 1.00 27.07 . 1 1416 ATOM C C VAL D 216 . −7.922 −14.012 44.186 1.00 27.26 . 1 1417 ATOM O O VAL D 216 . −6.944 −13.308 44.402 1.00 27.63 . 1 1418 ATOM C CB VAL D 216 . −8.714 −12.814 42.134 1.00 26.04 . 1 1419 ATOM C CG1 VAL D 216 . −8.024 −13.838 41.256 1.00 27.16 . 1 1420 ATOM C CG2 VAL D 216 . −9.966 −12.254 41.426 1.00 28.40 . 1 1421 ATOM N N GLY D 217 . −7.989 −15.291 44.544 1.00 28.05 . 1 1422 ATOM C CA GLY D 217 . −6.897 −15.899 45.291 1.00 28.81 . 1 1423 ATOM C C GLY D 217 . −7.047 −15.369 46.707 1.00 28.76 . 1 1424 ATOM O O GLY D 217 . −6.061 −15.080 47.395 1.00 29.80 . 1 1425 ATOM N N GLY D 218 . −8.303 −15.243 47.129 1.00 28.32 . 1 1426 ATOM C CA GLY D 218 . −8.626 −14.719 48.445 1.00 28.54 . 1 1427 ATOM C C GLY D 218 . −8.254 −15.581 49.639 1.00 31.43 . 1 1428 ATOM O O GLY D 218 . −8.164 −15.077 50.759 1.00 32.41 . 1 1429 ATOM N N GLY D 219 . −8.038 −16.870 49.412 1.00 30.94 . 1 1430 ATOM C CA GLY D 219 . −7.684 −17.757 50.501 1.00 32.94 . 1 1431 ATOM C C GLY D 219 . −8.868 −18.181 51.358 1.00 35.22 . 1 1432 ATOM O O GLY D 219 . −9.871 −18.700 50.854 1.00 35.41 . 1 1433 ATOM N N SER D 220 . −8.747 −17.948 52.662 1.00 33.22 . 1 1434 ATOM C CA SER D 220 . −9.773 −18.317 53.630 1.00 32.13 . 1 1435 ATOM C C SER D 220 . −10.967 −17.375 53.626 1.00 30.69 . 1 1436 ATOM O O SER D 220 . −12.035 −17.718 54.129 1.00 29.44 . 1 1437 ATOM C CB SER D 220 . −9.171 −18.326 55.035 1.00 33.10 . 1 1438 ATOM O OG SER D 220 . −8.852 −17.003 55.439 1.00 33.96 . 1 1439 ATOM N N GLY D 221 . −10.776 −16.184 53.070 1.00 30.85 . 1 1440 ATOM C CA GLY D 221 . −11.849 −15.211 53.042 1.00 30.41 . 1 1441 ATOM C C GLY D 221 . −11.795 −14.246 54.214 1.00 30.92 . 1 1442 ATOM O O GLY D 221 . −12.639 −13.360 54.337 1.00 30.10 . 1 1443 ATOM N N ARG D 222 . −10.801 −14.394 55.080 1.00 31.01 . 1 1444 ATOM C CA ARG D 222 . −10.715 −13.499 56.234 1.00 33.18 . 1 1445 ATOM C C ARG D 222 . −10.458 −12.048 55.827 1.00 30.51 . 1 1446 ATOM O O ARG D 222 . −10.940 −11.128 56.484 1.00 29.92 . 1 1447 ATOM C CB ARG D 222 . −9.641 −13.983 57.209 1.00 35.46 . 1 1448 ATOM C CG ARG D 222 . −10.035 −15.261 57.947 1.00 43.03 . 1 1449 ATOM C CD ARG D 222 . −11.242 −15.046 58.869 1.00 47.19 . 1 1450 ATOM N NE ARG D 222 . −11.683 −16.295 59.494 1.00 50.28 . 1 1451 ATOM C CZ ARG D 222 . −12.597 −16.378 60.458 1.00 51.79 . 1 1452 ATOM N NH1 ARG D 222 . −13.180 −15.281 60.924 1.00 50.98 . 1 1453 ATOM N NH2 ARG D 222 . −12.931 −17.564 60.957 1.00 51.86 . 1 1454 ATOM N N ASN D 223 . −9.717 −11.843 54.742 1.00 30.85 . 1 1455 ATOM C CA ASN D 223 . −9.449 −10.484 54.288 1.00 30.91 . 1 1456 ATOM C C ASN D 223 . −10.725 −9.815 53.808 1.00 32.90 . 1 1457 ATOM O O ASN D 223 . −10.938 −8.630 54.073 1.00 32.88 . 1 1458 ATOM C CB ASN D 223 . −8.374 −10.469 53.205 1.00 31.14 . 1 1459 ATOM C CG ASN D 223 . −7.005 −10.820 53.756 1.00 33.26 . 1 1460 ATOM O OD1 ASN D 223 . −6.738 −10.634 54.952 1.00 33.17 . 1 1461 ATOM N ND2 ASN D 223 . −6.127 −11.310 52.897 1.00 32.93 . 1 1462 ATOM N N LEU D 224 . −11.582 −10.560 53.109 1.00 31.37 . 1 1463 ATOM C CA LEU D 224 . −12.851 −9.990 52.667 1.00 32.53 . 1 1464 ATOM C C LEU D 224 . −13.693 −9.663 53.891 1.00 33.17 . 1 1465 ATOM O O LEU D 224 . −14.355 −8.629 53.938 1.00 34.18 . 1 1466 ATOM C CB LEU D 224 . −13.628 −10.966 51.772 1.00 32.99 . 1 1467 ATOM C CG LEU D 224 . −13.473 −10.781 50.267 1.00 35.50 . 1 1468 ATOM C CD1 LEU D 224 . −14.371 −11.771 49.528 1.00 33.83 . 1 1469 ATOM C CD2 LEU D 224 . −13.846 −9.343 49.893 1.00 35.32 . 1 1470 ATOM N N GLU D 225 . −13.669 −10.550 54.883 1.00 32.24 . 1 1471 ATOM C CA GLU D 225 . −14.438 −10.345 56.104 1.00 33.14 . 1 1472 ATOM C C GLU D 225 . −14.100 −8.983 56.713 1.00 33.96 . 1 1473 ATOM O O GLU D 225 . −14.987 −8.257 57.156 1.00 35.12 . 1 1474 ATOM C CB GLU D 225 . −14.142 −11.465 57.109 1.00 33.50 . 1 1475 ATOM C CG GLU D 225 . −14.815 −11.291 58.457 1.00 36.30 . 1 1476 ATOM C CD GLU D 225 . −14.621 −12.491 59.375 1.00 36.70 . 1 1477 ATOM O OE1 GLU D 225 . −13.477 −12.978 59.493 1.00 37.30 . 1 1478 ATOM O OE2 GLU D 225 . −15.616 −12.937 59.986 1.00 38.86 . 1 1479 ATOM N N LEU D 226 . −12.815 −8.640 56.726 1.00 35.54 . 1 1480 ATOM C CA LEU D 226 . −12.378 −7.357 57.267 1.00 36.71 . 1 1481 ATOM C C LEU D 226 . −12.886 −6.206 56.403 1.00 37.55 . 1 1482 ATOM O O LEU D 226 . −13.348 −5.189 56.923 1.00 38.12 . 1 1483 ATOM C CB LEU D 226 . −10.853 −7.307 57.349 1.00 36.67 . 1 1484 ATOM C CG LEU D 226 . −10.195 −8.155 58.436 1.00 37.87 . 1 1485 ATOM C CD1 LEU D 226 . −8.699 −8.159 58.233 1.00 37.50 . 1 1486 ATOM C CD2 LEU D 226 . −10.557 −7.612 59.821 1.00 37.05 . 1 1487 ATOM N N ILE D 227 . −12.801 −6.373 55.086 1.00 37.06 . 1 1488 ATOM C CA ILE D 227 . −13.255 −5.346 54.151 1.00 37.48 . 1 1489 ATOM C C ILE D 227 . −14.749 −5.099 54.311 1.00 39.01 . 1 1490 ATOM O O ILE D 227 . −15.185 −3.962 54.514 1.00 38.78 . 1 1491 ATOM C CB ILE D 227 . −12.998 −5.759 52.683 1.00 37.38 . 1 1492 ATOM C CG1 ILE D 227 . −11.508 −6.023 52.458 1.00 36.61 . 1 1493 ATOM C CG2 ILE D 227 . −13.508 −4.679 51.740 1.00 37.37 . 1 1494 ATOM C CD1 ILE D 227 . −10.610 −4.911 52.917 1.00 40.43 . 1 1495 ATOM N N ILE D 228 . −15.529 −6.172 54.212 1.00 38.38 . 1 1496 ATOM C CA ILE D 228 . −16.976 −6.090 54.336 1.00 39.42 . 1 1497 ATOM C C ILE D 228 . −17.398 −5.615 55.723 1.00 39.17 . 1 1498 ATOM O O ILE D 228 . −18.483 −5.066 55.898 1.00 40.19 . 1 1499 ATOM C CB ILE D 228 . −17.620 −7.456 54.020 1.00 40.25 . 1 1500 ATOM C CG1 ILE D 228 . −17.407 −7.782 52.541 1.00 40.81 . 1 1501 ATOM C CG2 ILE D 228 . −19.102 −7.433 54.343 1.00 42.16 . 1 1502 ATOM C CD1 ILE D 228 . −17.908 −9.150 52.131 1.00 42.89 . 1 1503 ATOM N N SER D 229 . −16.528 −5.824 56.703 1.00 41.56 . 1 1504 ATOM C CA SER D 229 . −16.792 −5.401 58.070 1.00 44.14 . 1 1505 ATOM C C SER D 229 . −16.862 −3.877 58.092 1.00 46.03 . 1 1506 ATOM O O SER D 229 . −17.700 −3.291 58.779 1.00 47.11 . 1 1507 ATOM C CB SER D 229 . −15.672 −5.893 58.991 1.00 45.84 . 1 1508 ATOM O OG SER D 229 . −15.921 −5.560 60.344 1.00 48.20 . 1 1509 ATOM N N LYS D 230 . −15.979 −3.240 57.328 1.00 46.67 . 1 1510 ATOM C CA LYS D 230 . −15.946 −1.784 57.249 1.00 47.10 . 1 1511 ATOM C C LYS D 230 . −16.877 −1.268 56.159 1.00 47.25 . 1 1512 ATOM O O LYS D 230 . −17.361 −0.139 56.232 1.00 47.41 . 1 1513 ATOM C CB LYS D 230 . −14.523 −1.297 56.975 1.00 47.42 . 1 1514 ATOM C CG LYS D 230 . −14.425 0.207 56.764 1.00 48.48 . 1 1515 ATOM C CD LYS D 230 . −12.983 0.683 56.756 1.00 48.50 . 1 1516 ATOM C CE LYS D 230 . −12.923 2.202 56.676 1.00 48.90 . 1 1517 ATOM N NZ LYS D 230 . −11.554 2.733 56.899 1.00 48.61 . 1 1518 ATOM N N TYR D 231 . −17.123 −2.096 55.146 1.00 46.79 . 1 1519 ATOM C CA TYR D 231 . −18.001 −1.713 54.044 1.00 47.52 . 1 1520 ATOM C C TYR D 231 . −19.127 −2.732 53.837 1.00 47.83 . 1 1521 ATOM O O TYR D 231 . −19.143 −3.473 52.853 1.00 47.24 . 1 1522 ATOM C CB TYR D 231 . −17.187 −1.548 52.759 1.00 46.59 . 1 1523 ATOM C CG TYR D 231 . −16.087 −0.515 52.879 1.00 48.12 . 1 1524 ATOM C CD1 TYR D 231 . −14.792 −0.882 53.246 1.00 47.30 . 1 1525 ATOM C CD2 TYR D 231 . −16.351 0.838 52.661 1.00 48.57 . 1 1526 ATOM C CE1 TYR D 231 . −13.785 0.073 53.393 1.00 47.85 . 1 1527 ATOM C CE2 TYR D 231 . −15.355 1.803 52.808 1.00 48.45 . 1 1528 ATOM C CZ TYR D 231 . −14.076 1.415 53.174 1.00 48.60 . 1 1529 ATOM O OH TYR D 231 . −13.094 2.371 53.322 1.00 48.21 . 1 1530 ATOM N N PRO D 232 . −20.094 −2.759 54.770 1.00 48.64 . 1 1531 ATOM C CA PRO D 232 . −21.277 −3.627 54.826 1.00 48.22 . 1 1532 ATOM C C PRO D 232 . −22.110 −3.763 53.551 1.00 48.51 . 1 1533 ATOM O O PRO D 232 . −22.767 −4.783 53.343 1.00 49.21 . 1 1534 ATOM C CB PRO D 232 . −22.087 −3.019 55.967 1.00 49.38 . 1 1535 ATOM C CG PRO D 232 . −21.034 −2.519 56.885 1.00 49.92 . 1 1536 ATOM C CD PRO D 232 . −20.075 −1.848 55.929 1.00 48.94 . 1 1537 ATOM N N LEU D 233 . −22.092 −2.745 52.700 1.00 47.47 . 1 1538 ATOM C CA LEU D 233 . −22.875 −2.788 51.474 1.00 47.09 . 1 1539 ATOM C C LEU D 233 . −22.232 −3.656 50.400 1.00 46.48 . 1 1540 ATOM O O LEU D 233 . −22.890 −4.060 49.438 1.00 46.50 . 1 1541 ATOM C CB LEU D 233 . −23.077 −1.372 50.929 1.00 49.72 . 1 1542 ATOM C CG LEU D 233 . −23.769 −0.363 51.852 1.00 50.91 . 1 1543 ATOM C CD1 LEU D 233 . −23.961 0.945 51.100 1.00 52.22 . 1 1544 ATOM C CD2 LEU D 233 . −25.113 −0.905 52.313 1.00 52.20 . 1 1545 ATOM N N ILE D 234 . −20.946 −3.945 50.560 1.00 43.92 . 1 1546 ATOM C CA ILE D 234 . −20.244 −4.762 49.579 1.00 41.58 . 1 1547 ATOM C C ILE D 234 . −20.588 −6.244 49.678 1.00 41.40 . 1 1548 ATOM O O ILE D 234 . −20.570 −6.830 50.762 1.00 40.60 . 1 1549 ATOM C CB ILE D 234 . −18.708 −4.624 49.715 1.00 40.81 . 1 1550 ATOM C CG1 ILE D 234 . −18.270 −3.210 49.329 1.00 39.33 . 1 1551 ATOM C CG2 ILE D 234 . −18.009 −5.659 48.833 1.00 38.99 . 1 1552 ATOM C CD1 ILE D 234 . −16.789 −2.946 49.527 1.00 37.33 . 1 1553 ATOM N N LYS D 235 . −20.913 −6.832 48.531 1.00 41.68 . 1 1554 ATOM C CA LYS D 235 . −21.210 −8.253 48.447 1.00 41.44 . 1 1555 ATOM C C LYS D 235 . −19.866 −8.889 48.094 1.00 39.45 . 1 1556 ATOM O O LYS D 235 . −19.280 −8.587 47.050 1.00 38.58 . 1 1557 ATOM C CB LYS D 235 . −22.228 −8.531 47.337 1.00 43.65 . 1 1558 ATOM C CG LYS D 235 . −23.611 −7.940 47.578 1.00 47.25 . 1 1559 ATOM C CD LYS D 235 . −24.252 −8.513 48.835 1.00 51.15 . 1 1560 ATOM C CE LYS D 235 . −25.616 −7.889 49.093 1.00 52.36 . 1 1561 ATOM N NZ LYS D 235 . −26.234 −8.388 50.356 1.00 54.54 . 1 1562 ATOM N N GLY D 236 . −19.375 −9.765 48.959 1.00 35.81 . 1 1563 ATOM C CA GLY D 236 . −18.090 −10.375 48.693 1.00 33.84 . 1 1564 ATOM C C GLY D 236 . −18.097 −11.760 48.088 1.00 31.44 . 1 1565 ATOM O O GLY D 236 . −18.952 −12.588 48.390 1.00 31.85 . 1 1566 ATOM N N ILE D 237 . −17.133 −11.997 47.209 1.00 31.35 . 1 1567 ATOM C CA ILE D 237 . −16.963 −13.296 46.580 1.00 31.70 . 1 1568 ATOM C C ILE D 237 . −15.511 −13.692 46.790 1.00 30.20 . 1 1569 ATOM O O ILE D 237 . −14.602 −13.103 46.204 1.00 30.28 . 1 1570 ATOM C CB ILE D 237 . −17.280 −13.266 45.062 1.00 32.25 . 1 1571 ATOM C CG1 ILE D 237 . −18.786 −13.070 44.854 1.00 32.97 . 1 1572 ATOM C CG2 ILE D 237 . −16.832 −14.576 44.407 1.00 31.96 . 1 1573 ATOM C CD1 ILE D 237 . −19.206 −13.023 43.395 1.00 34.90 . 1 1574 ATOM N N ASN D 238 . −15.301 −14.671 47.664 1.00 30.36 . 1 1575 ATOM C CA ASN D 238 . −13.963 −15.165 47.953 1.00 29.46 . 1 1576 ATOM C C ASN D 238 . −13.693 −16.263 46.931 1.00 28.45 . 1 1577 ATOM O O ASN D 238 . −14.337 −17.314 46.950 1.00 28.80 . 1 1578 ATOM C CB ASN D 238 . −13.907 −15.734 49.371 1.00 29.85 . 1 1579 ATOM C CG ASN D 238 . −12.517 −16.187 49.757 1.00 31.61 . 1 1580 ATOM O OD1 ASN D 238 . −12.338 −17.282 50.282 1.00 33.26 . 1 1581 ATOM N ND2 ASN D 238 . −11.525 −15.341 49.502 1.00 29.78 . 1 1582 ATOM N N PHE D 239 . −12.727 −16.012 46.057 1.00 26.96 . 1 1583 ATOM C CA PHE D 239 . −12.390 −16.924 44.975 1.00 27.94 . 1 1584 ATOM C C PHE D 239 . −11.009 −17.534 45.101 1.00 28.26 . 1 1585 ATOM O O PHE D 239 . −10.009 −16.819 45.210 1.00 30.03 . 1 1586 ATOM C CB PHE D 239 . −12.494 −16.164 43.650 1.00 29.07 . 1 1587 ATOM C CG PHE D 239 . −12.246 −17.009 42.437 1.00 29.44 . 1 1588 ATOM C CD1 PHE D 239 . −13.099 −18.062 42.122 1.00 32.74 . 1 1589 ATOM C CD2 PHE D 239 . −11.170 −16.736 41.596 1.00 32.18 . 1 1590 ATOM C CE1 PHE D 239 . −12.887 −18.838 40.981 1.00 30.68 . 1 1591 ATOM C CE2 PHE D 239 . −10.944 −17.504 40.448 1.00 32.15 . 1 1592 ATOM C CZ PHE D 239 . −11.809 −18.559 40.143 1.00 33.86 . 1 1593 ATOM N N ASP D 240 . −10.953 −18.860 45.058 1.00 29.22 . 1 1594 ATOM C CA ASP D 240 . −9.682 −19.559 45.162 1.00 30.54 . 1 1595 ATOM C C ASP D 240 . −9.839 −20.987 44.633 1.00 32.07 . 1 1596 ATOM O O ASP D 240 . −10.921 −21.379 44.174 1.00 32.83 . 1 1597 ATOM C CB ASP D 240 . −9.226 −19.574 46.630 1.00 28.87 . 1 1598 ATOM C CG ASP D 240 . −7.718 −19.574 46.773 1.00 31.79 . 1 1599 ATOM O OD1 ASP D 240 . −7.077 −20.537 46.300 1.00 31.79 . 1 1600 ATOM O OD2 ASP D 240 . −7.170 −18.611 47.356 1.00 30.66 . 1 1601 ATOM N N LEU D 241 . −8.761 −21.759 44.703 1.00 33.76 . 1 1602 ATOM C CA LEU D 241 . −8.768 −23.148 44.235 1.00 34.47 . 1 1603 ATOM C C LEU D 241 . −9.792 −23.992 44.984 1.00 36.26 . 1 1604 ATOM O O LEU D 241 . −10.035 −23.787 46.175 1.00 34.67 . 1 1605 ATOM C CB LEU D 241 . −7.382 −23.768 44.415 1.00 34.81 . 1 1606 ATOM C CG LEU D 241 . −6.270 −23.155 43.568 1.00 34.80 . 1 1607 ATOM C CD1 LEU D 241 . −4.911 −23.591 44.088 1.00 35.62 . 1 1608 ATOM C CD2 LEU D 241 . −6.467 −23.575 42.125 1.00 36.51 . 1 1609 ATOM N N PRO D 242 . −10.408 −24.961 44.289 1.00 37.69 . 1 1610 ATOM C CA PRO D 242 . −11.407 −25.834 44.906 1.00 38.03 . 1 1611 ATOM C C PRO D 242 . −10.930 −26.430 46.229 1.00 37.22 . 1 1612 ATOM O O PRO D 242 . −11.677 −26.466 47.206 1.00 37.42 . 1 1613 ATOM C CB PRO D 242 . −11.631 −26.898 43.830 1.00 38.35 . 1 1614 ATOM C CG PRO D 242 . −11.490 −26.104 42.574 1.00 39.10 . 1 1615 ATOM C CD PRO D 242 . −10.256 −25.275 42.855 1.00 38.31 . 1 1616 ATOM N N GLN D 243 . −9.682 −26.888 46.257 1.00 38.57 . 1 1617 ATOM C CA GLN D 243 . −9.115 −27.498 47.454 1.00 39.67 . 1 1618 ATOM C C GLN D 243 . −8.968 −26.513 48.613 1.00 40.10 . 1 1619 ATOM O O GLN D 243 . −8.902 −26.909 49.779 1.00 39.50 . 1 1620 ATOM C CB GLN D 243 . −7.755 −28.133 47.135 1.00 41.57 . 1 1621 ATOM C CG GLN D 243 . −6.834 −27.272 46.273 1.00 42.71 . 1 1622 ATOM C CD GLN D 243 . −6.985 −27.545 44.780 1.00 43.39 . 1 1623 ATOM O OE1 GLN D 243 . −8.088 −27.510 44.231 1.00 41.83 . 1 1624 ATOM N NE2 GLN D 243 . −5.866 −27.812 44.117 1.00 43.67 . 1 1625 ATOM N N VAL D 244 . −8.911 −25.226 48.295 1.00 39.27 . 1 1626 ATOM C CA VAL D 244 . −8.785 −24.222 49.339 1.00 37.50 . 1 1627 ATOM C C VAL D 244 . −10.172 −23.870 49.867 1.00 36.59 . 1 1628 ATOM O O VAL D 244 . −10.412 −23.883 51.074 1.00 36.14 . 1 1629 ATOM C CB VAL D 244 . −8.103 −22.944 48.806 1.00 36.57 . 1 1630 ATOM C CG1 VAL D 244 . −8.019 −21.898 49.915 1.00 36.95 . 1 1631 ATOM C CG2 VAL D 244 . −6.712 −23.280 48.288 1.00 36.36 . 1 1632 ATOM N N ILE D 245 . −11.087 −23.574 48.949 1.00 35.77 . 1 1633 ATOM C CA ILE D 245 . −12.454 −23.204 49.301 1.00 35.72 . 1 1634 ATOM C C ILE D 245 . −13.177 −24.246 50.157 1.00 37.99 . 1 1635 ATOM O O ILE D 245 . −13.986 −23.896 51.021 1.00 36.95 . 1 1636 ATOM C CB ILE D 245 . −13.281 −22.909 48.016 1.00 35.84 . 1 1637 ATOM C CG1 ILE D 245 . −12.691 −21.693 47.293 1.00 34.28 . 1 1638 ATOM C CG2 ILE D 245 . −14.746 −22.665 48.358 1.00 36.70 . 1 1639 ATOM C CD1 ILE D 245 . −12.621 −20.437 48.151 1.00 34.53 . 1 1640 ATOM N N GLU D 246 . −12.878 −25.524 49.941 1.00 39.99 . 1 1641 ATOM C CA GLU D 246 . −13.536 −26.573 50.712 1.00 42.91 . 1 1642 ATOM C C GLU D 246 . −13.167 −26.515 52.197 1.00 42.44 . 1 1643 ATOM O O GLU D 246 . −13.858 −27.090 53.037 1.00 41.77 . 1 1644 ATOM C CB GLU D 246 . −13.210 −27.955 50.130 1.00 46.46 . 1 1645 ATOM C CG GLU D 246 . −11.788 −28.439 50.352 1.00 52.65 . 1 1646 ATOM C CD GLU D 246 . −11.546 −29.824 49.757 1.00 56.15 . 1 1647 ATOM O OE1 GLU D 246 . −12.381 −30.726 49.991 1.00 57.44 . 1 1648 ATOM O OE2 GLU D 246 . −10.519 −30.016 49.065 1.00 58.88 . 1 1649 ATOM N N ASN D 247 . −12.091 −25.805 52.523 1.00 42.15 . 1 1650 ATOM C CA ASN D 247 . −11.660 −25.673 53.916 1.00 42.01 . 1 1651 ATOM C C ASN D 247 . −11.948 −24.279 54.461 1.00 40.41 . 1 1652 ATOM O O ASN D 247 . −11.601 −23.966 55.599 1.00 39.36 . 1 1653 ATOM C CB ASN D 247 . −10.162 −25.966 54.043 1.00 45.09 . 1 1654 ATOM C CG ASN D 247 . −9.824 −27.400 53.712 1.00 46.79 . 1 1655 ATOM O OD1 ASN D 247 . −10.291 −28.328 54.375 1.00 48.87 . 1 1656 ATOM N ND2 ASN D 247 . −9.015 −27.593 52.678 1.00 48.93 . 1 1657 ATOM N N ALA D 248 . −12.572 −23.443 53.639 1.00 38.77 . 1 1658 ATOM C CA ALA D 248 . −12.904 −22.083 54.046 1.00 36.89 . 1 1659 ATOM C C ALA D 248 . −14.146 −22.084 54.923 1.00 34.34 . 1 1660 ATOM O O ALA D 248 . −15.163 −22.688 54.586 1.00 34.37 . 1 1661 ATOM C CB ALA D 248 . −13.130 −21.201 52.817 1.00 37.40 . 1 1662 ATOM N N PRO D 249 . −14.081 −21.394 56.065 1.00 34.10 . 1 1663 ATOM C CA PRO D 249 . −15.212 −21.324 56.986 1.00 33.71 . 1 1664 ATOM C C PRO D 249 . −16.342 −20.457 56.447 1.00 32.34 . 1 1665 ATOM O O PRO D 249 . −16.120 −19.557 55.639 1.00 31.08 . 1 1666 ATOM C CB PRO D 249 . −14.585 −20.722 58.239 1.00 35.23 . 1 1667 ATOM C CG PRO D 249 . −13.610 −19.740 57.648 1.00 35.18 . 1 1668 ATOM C CD PRO D 249 . −12.953 −20.581 56.561 1.00 36.72 . 1 1669 ATOM N N PRO D 250 . −17.579 −20.730 56.877 1.00 32.13 . 1 1670 ATOM C CA PRO D 250 . −18.689 −19.908 56.389 1.00 32.56 . 1 1671 ATOM C C PRO D 250 . −18.510 −18.503 56.981 1.00 33.13 . 1 1672 ATOM O O PRO D 250 . −18.118 −18.357 58.146 1.00 32.11 . 1 1673 ATOM C CB PRO D 250 . −19.924 −20.609 56.958 1.00 32.58 . 1 1674 ATOM C CG PRO D 250 . −19.463 −22.031 57.182 1.00 35.45 . 1 1675 ATOM C CD PRO D 250 . −18.062 −21.853 57.697 1.00 33.06 . 1 1676 ATOM N N LEU D 251 . −18.786 −17.483 56.179 1.00 32.13 . 1 1677 ATOM C CA LEU D 251 . −18.660 −16.102 56.628 1.00 33.76 . 1 1678 ATOM C C LEU D 251 . −19.851 −15.301 56.124 1.00 33.63 . 1 1679 ATOM O O LEU D 251 . −20.275 −15.442 54.974 1.00 35.87 . 1 1680 ATOM C CB LEU D 251 . −17.359 −15.480 56.104 1.00 33.78 . 1 1681 ATOM C CG LEU D 251 . −16.015 −16.086 56.525 1.00 33.10 . 1 1682 ATOM C CD1 LEU D 251 . −14.919 −15.550 55.616 1.00 33.33 . 1 1683 ATOM C CD2 LEU D 251 . −15.721 −15.755 57.982 1.00 34.60 . 1 1684 ATOM N N SER D 252 . −20.384 −14.459 56.998 1.00 35.38 . 1 1685 ATOM C CA SER D 252 . −21.531 −13.623 56.680 1.00 36.76 . 1 1686 ATOM C C SER D 252 . −21.237 −12.660 55.533 1.00 35.94 . 1 1687 ATOM O O SER D 252 . −20.188 −12.022 55.502 1.00 34.90 . 1 1688 ATOM C CB SER D 252 . −21.947 −12.833 57.929 1.00 38.29 . 1 1689 ATOM O OG SER D 252 . −23.005 −11.939 57.637 1.00 45.57 . 1 1690 ATOM N N GLY D 253 . −22.172 −12.569 54.590 1.00 35.80 . 1 1691 ATOM C CA GLY D 253 . −22.017 −11.665 53.461 1.00 35.60 . 1 1692 ATOM C C GLY D 253 . −20.929 −12.019 52.463 1.00 35.15 . 1 1693 ATOM O O GLY D 253 . −20.540 −11.182 51.642 1.00 35.64 . 1 1694 ATOM N N ILE D 254 . −20.432 −13.250 52.519 1.00 34.61 . 1 1695 ATOM C CA ILE D 254 . −19.386 −13.677 51.599 1.00 32.77 . 1 1696 ATOM C C ILE D 254 . −19.715 −15.010 50.952 1.00 34.12 . 1 1697 ATOM O O ILE D 254 . −20.119 −15.957 51.626 1.00 34.77 . 1 1698 ATOM C CB ILE D 254 . −18.009 −13.794 52.316 1.00 31.17 . 1 1699 ATOM C CG1 ILE D 254 . −17.538 −12.400 52.752 1.00 29.60 . 1 1700 ATOM C CG2 ILE D 254 . −16.984 −14.449 51.388 1.00 29.13 . 1 1701 ATOM C CD1 ILE D 254 . −16.328 −12.394 53.654 1.00 28.74 . 1 1702 ATOM N N GLU D 255 . −19.540 −15.072 49.639 1.00 34.09 . 1 1703 ATOM C CA GLU D 255 . −19.798 −16.293 48.895 1.00 36.68 . 1 1704 ATOM C C GLU D 255 . −18.474 −16.911 48.454 1.00 34.89 . 1 1705 ATOM O O GLU D 255 . −17.693 −16.288 47.745 1.00 35.27 . 1 1706 ATOM C CB GLU D 255 . −20.666 −15.999 47.665 1.00 39.34 . 1 1707 ATOM C CG GLU D 255 . −21.083 −17.249 46.890 1.00 44.96 . 1 1708 ATOM C CD GLU D 255 . −21.867 −16.929 45.625 1.00 47.87 . 1 1709 ATOM O OE1 GLU D 255 . −22.875 −16.196 45.710 1.00 50.68 . 1 1710 ATOM O OE2 GLU D 255 . −21.478 −17.417 44.543 1.00 49.76 . 1 1711 ATOM N N HIS D 256 . −18.216 −18.134 48.896 1.00 35.16 . 1 1712 ATOM C CA HIS D 256 . −16.996 −18.827 48.516 1.00 34.17 . 1 1713 ATOM C C HIS D 256 . −17.213 −19.454 47.140 1.00 35.95 . 1 1714 ATOM O O HIS D 256 . −18.250 −20.071 46.888 1.00 35.76 . 1 1715 ATOM C CB HIS D 256 . −16.670 −19.922 49.529 1.00 33.82 . 1 1716 ATOM C CG HIS D 256 . −16.240 −19.401 50.864 1.00 33.13 . 1 1717 ATOM N ND1 HIS D 256 . −15.090 −18.659 51.036 1.00 33.03 . 1 1718 ATOM C CD2 HIS D 256 . −16.800 −19.520 52.091 1.00 29.57 . 1 1719 ATOM C CE1 HIS D 256 . −14.961 −18.344 52.313 1.00 31.35 . 1 1720 ATOM N NE2 HIS D 256 . −15.985 −18.853 52.974 1.00 33.61 . 1 1721 ATOM N N VAL D 257 . −16.239 −19.283 46.253 1.00 35.16 . 1 1722 ATOM C CA VAL D 257 . −16.324 −19.841 44.909 1.00 35.25 . 1 1723 ATOM C C VAL D 257 . −15.018 −20.516 44.534 1.00 35.58 . 1 1724 ATOM O O VAL D 257 . −13.981 −19.864 44.456 1.00 34.93 . 1 1725 ATOM C CB VAL D 257 . −16.618 −18.746 43.860 1.00 35.53 . 1 1726 ATOM C CG1 VAL D 257 . −16.541 −19.340 42.452 1.00 33.32 . 1 1727 ATOM C CG2 VAL D 257 . −17.991 −18.139 44.117 1.00 33.39 . 1 1728 ATOM N N GLY D 258 . −15.074 −21.824 44.304 1.00 36.13 . 1 1729 ATOM C CA GLY D 258 . −13.878 −22.553 43.925 1.00 37.07 . 1 1730 ATOM C C GLY D 258 . −13.687 −22.487 42.425 1.00 38.12 . 1 1731 ATOM O O GLY D 258 . −14.659 −22.544 41.672 1.00 38.86 . 1 1732 ATOM N N GLY D 259 . −12.445 −22.359 41.977 1.00 36.64 . 1 1733 ATOM C CA GLY D 259 . −12.203 −22.289 40.548 1.00 36.33 . 1 1734 ATOM C C GLY D 259 . −10.739 −22.173 40.184 1.00 35.55 . 1 1735 ATOM O O GLY D 259 . −9.867 −22.563 40.957 1.00 33.22 . 1 1736 ATOM N N ASP D 260 . −10.475 −21.637 38.996 1.00 35.75 . 1 1737 ATOM C CA ASP D 260 . −9.115 −21.458 38.500 1.00 35.44 . 1 1738 ATOM C C ASP D 260 . −9.007 −20.118 37.773 1.00 35.78 . 1 1739 ATOM O O ASP D 260 . −9.584 −19.932 36.700 1.00 35.99 . 1 1740 ATOM C CB ASP D 260 . −8.753 −22.621 37.568 1.00 35.76 . 1 1741 ATOM C CG ASP D 260 . −7.415 −22.434 36.885 1.00 35.67 . 1 1742 ATOM O OD1 ASP D 260 . −6.641 −21.549 37.304 1.00 37.30 . 1 1743 ATOM O OD2 ASP D 260 . −7.131 −23.180 35.926 1.00 34.76 . 1 1744 ATOM N N MET D 261 . −8.273 −19.185 38.377 1.00 33.63 . 1 1745 ATOM C CA MET D 261 . −8.084 −17.847 37.827 1.00 32.80 . 1 1746 ATOM C C MET D 261 . −7.452 −17.829 36.437 1.00 34.01 . 1 1747 ATOM O O MET D 261 . −7.547 −16.833 35.718 1.00 34.33 . 1 1748 ATOM C CB MET D 261 . −7.238 −17.003 38.784 1.00 31.30 . 1 1749 ATOM C CG MET D 261 . −5.844 −17.533 39.017 1.00 30.59 . 1 1750 ATOM S SD MET D 261 . −4.993 −16.571 40.297 1.00 29.09 . 1 1751 ATOM C CE MET D 261 . −3.320 −17.192 40.098 1.00 27.53 . 1 1752 ATOM N N PHE D 262 . −6.790 −18.917 36.067 1.00 34.81 . 1 1753 ATOM C CA PHE D 262 . −6.180 −19.000 34.753 1.00 36.27 . 1 1754 ATOM C C PHE D 262 . −7.257 −19.326 33.721 1.00 36.88 . 1 1755 ATOM O O PHE D 262 . −7.065 −19.100 32.524 1.00 37.27 . 1 1756 ATOM C CB PHE D 262 . −5.082 −20.069 34.730 1.00 37.18 . 1 1757 ATOM C CG PHE D 262 . −3.837 −19.676 35.477 1.00 36.52 . 1 1758 ATOM C CD1 PHE D 262 . −3.503 −20.293 36.679 1.00 37.73 . 1 1759 ATOM C CD2 PHE D 262 . −3.008 −18.675 34.989 1.00 35.95 . 1 1760 ATOM C CE1 PHE D 262 . −2.362 −19.916 37.381 1.00 36.44 . 1 1761 ATOM C CE2 PHE D 262 . −1.864 −18.290 35.684 1.00 37.38 . 1 1762 ATOM C CZ PHE D 262 . −1.542 −18.914 36.885 1.00 35.56 . 1 1763 ATOM N N ALA D 263 . −8.386 −19.853 34.188 1.00 36.80 . 1 1764 ATOM C CA ALA D 263 . −9.496 −20.195 33.298 1.00 39.97 . 1 1765 ATOM C C ALA D 263 . −10.495 −19.045 33.215 1.00 40.00 . 1 1766 ATOM O O ALA D 263 . −10.823 −18.575 32.125 1.00 40.18 . 1 1767 ATOM C CB ALA D 263 . −10.197 −21.458 33.786 1.00 39.67 . 1 1768 ATOM N N SER D 264 . −10.973 −18.596 34.372 1.00 39.15 . 1 1769 ATOM C CA SER D 264 . −11.936 −17.499 34.440 1.00 40.06 . 1 1770 ATOM C C SER D 264 . −12.144 −17.041 35.881 1.00 39.73 . 1 1771 ATOM O O SER D 264 . −12.014 −17.827 36.819 1.00 40.56 . 1 1772 ATOM C CB SER D 264 . −13.282 −17.934 33.855 1.00 39.57 . 1 1773 ATOM O OG SER D 264 . −13.818 −19.025 34.585 1.00 42.10 . 1 1774 ATOM N N VAL D 265 . −12.489 −15.768 36.037 1.00 39.55 . 1 1775 ATOM C CA VAL D 265 . −12.716 −15.162 37.346 1.00 39.53 . 1 1776 ATOM C C VAL D 265 . −14.174 −14.729 37.505 1.00 40.32 . 1 1777 ATOM O O VAL D 265 . −14.800 −14.270 36.551 1.00 40.33 . 1 1778 ATOM C CB VAL D 265 . −11.808 −13.924 37.521 1.00 38.02 . 1 1779 ATOM C CG1 VAL D 265 . −12.186 −13.158 38.769 1.00 40.28 . 1 1780 ATOM C CG2 VAL D 265 . −10.354 −14.361 37.584 1.00 38.21 . 1 1781 ATOM N N PRO D 266 . −14.736 −14.881 38.713 1.00 40.54 . 1 1782 ATOM C CA PRO D 266 . −16.126 −14.482 38.945 1.00 40.80 . 1 1783 ATOM C C PRO D 266 . −16.341 −13.022 38.572 1.00 40.61 . 1 1784 ATOM O O PRO D 266 . −15.435 −12.197 38.709 1.00 39.44 . 1 1785 ATOM C CB PRO D 266 . −16.305 −14.728 40.440 1.00 41.18 . 1 1786 ATOM C CG PRO D 266 . −15.436 −15.916 40.678 1.00 40.34 . 1 1787 ATOM C CD PRO D 266 . −14.186 −15.564 39.899 1.00 41.18 . 1 1788 ATOM N N GLN D 267 . −17.540 −12.705 38.096 1.00 40.00 . 1 1789 ATOM C CA GLN D 267 . −17.866 −11.339 37.704 1.00 40.34 . 1 1790 ATOM C C GLN D 267 . −18.071 −10.416 38.896 1.00 38.04 . 1 1791 ATOM O O GLN D 267 . −18.569 −10.827 39.940 1.00 38.41 . 1 1792 ATOM C CB GLN D 267 . −19.125 −11.322 36.835 1.00 41.85 . 1 1793 ATOM C CG GLN D 267 . −18.916 −11.875 35.440 1.00 46.31 . 1 1794 ATOM C CD GLN D 267 . −20.175 −11.810 34.595 1.00 49.37 . 1 1795 ATOM O OE1 GLN D 267 . −21.163 −12.491 34.877 1.00 51.11 . 1 1796 ATOM N NE2 GLN D 267 . −20.147 −10.984 33.555 1.00 49.75 . 1 1797 ATOM N N GLY D 268 . −17.683 −9.160 38.724 1.00 38.03 . 1 1798 ATOM C CA GLY D 268 . −17.836 −8.174 39.776 1.00 38.26 . 1 1799 ATOM C C GLY D 268 . −17.379 −6.840 39.231 1.00 38.18 . 1 1800 ATOM O O GLY D 268 . −16.772 −6.799 38.166 1.00 39.25 . 1 1801 ATOM N N ASP D 269 . −17.668 −5.749 39.934 1.00 38.67 . 1 1802 ATOM C CA ASP D 269 . −17.239 −4.436 39.467 1.00 39.09 . 1 1803 ATOM C C ASP D 269 . −15.872 −4.073 40.032 1.00 39.16 . 1 1804 ATOM O O ASP D 269 . −15.286 −3.046 39.680 1.00 39.37 . 1 1805 ATOM C CB ASP D 269 . −18.275 −3.360 39.824 1.00 40.54 . 1 1806 ATOM C CG ASP D 269 . −18.865 −3.537 41.209 1.00 42.38 . 1 1807 ATOM O OD1 ASP D 269 . −18.489 −2.772 42.125 1.00 44.67 . 1 1808 ATOM O OD2 ASP D 269 . −19.713 −4.441 41.379 1.00 43.52 . 1 1809 ATOM N N ALA D 270 . −15.364 −4.931 40.910 1.00 37.02 . 1 1810 ATOM C CA ALA D 270 . −14.060 −4.714 41.509 1.00 35.06 . 1 1811 ATOM C C ALA D 270 . −13.494 −6.053 41.918 1.00 33.82 . 1 1812 ATOM O O ALA D 270 . −14.229 −6.929 42.368 1.00 34.60 . 1 1813 ATOM C CB ALA D 270 . −14.175 −3.803 42.727 1.00 34.61 . 1 1814 ATOM N N MET D 271 . −12.186 −6.207 41.749 1.00 33.30 . 1 1815 ATOM C CA MET D 271 . −11.505 −7.435 42.118 1.00 33.10 . 1 1816 ATOM C C MET D 271 . −10.219 −7.067 42.807 1.00 32.58 . 1 1817 ATOM O O MET D 271 . −9.486 −6.195 42.344 1.00 33.70 . 1 1818 ATOM C CB MET D 271 . −11.178 −8.261 40.886 1.00 31.43 . 1 1819 ATOM C CG MET D 271 . −12.403 −8.668 40.099 1.00 33.42 . 1 1820 ATOM S SD MET D 271 . −11.948 −9.152 38.439 1.00 36.92 . 1 1821 ATOM C CE MET D 271 . −13.616 −9.368 37.715 1.00 34.12 . 1 1822 ATOM N N ILE D 272 . −9.934 −7.743 43.911 1.00 30.88 . 1 1823 ATOM C CA ILE D 272 . −8.714 −7.464 44.638 1.00 28.69 . 1 1824 ATOM C C ILE D 272 . −7.816 −8.690 44.608 1.00 29.57 . 1 1825 ATOM O O ILE D 272 . −8.280 −9.817 44.762 1.00 28.39 . 1 1826 ATOM C CB ILE D 272 . −9.026 −7.035 46.104 1.00 29.28 . 1 1827 ATOM C CG1 ILE D 272 . −7.720 −6.792 46.867 1.00 31.27 . 1 1828 ATOM C CG2 ILE D 272 . −9.901 −8.076 46.787 1.00 30.05 . 1 1829 ATOM C CD1 ILE D 272 . −7.924 −6.243 48.275 1.00 32.27 . 1 1830 ATOM N N LEU D 273 . −6.537 −8.461 44.340 1.00 28.10 . 1 1831 ATOM C CA LEU D 273 . −5.554 −9.528 44.320 1.00 28.01 . 1 1832 ATOM C C LEU D 273 . −4.464 −9.095 45.271 1.00 26.41 . 1 1833 ATOM O O LEU D 273 . −3.695 −8.189 44.968 1.00 26.17 . 1 1834 ATOM C CB LEU D 273 . −4.955 −9.727 42.929 1.00 27.03 . 1 1835 ATOM C CG LEU D 273 . −5.778 −10.492 41.888 1.00 26.59 . 1 1836 ATOM C CD1 LEU D 273 . −6.922 −9.616 41.381 1.00 28.18 . 1 1837 ATOM C CD2 LEU D 273 . −4.873 −10.887 40.741 1.00 29.38 . 1 1838 ATOM N N LYS D 274 . −4.411 −9.738 46.427 1.00 26.26 . 1 1839 ATOM C CA LYS D 274 . −3.402 −9.408 47.418 1.00 24.21 . 1 1840 ATOM C C LYS D 274 . −2.415 −10.553 47.555 1.00 25.78 . 1 1841 ATOM O O LYS D 274 . −2.799 −11.681 47.880 1.00 26.13 . 1 1842 ATOM C CB LYS D 274 . −4.069 −9.132 48.759 1.00 27.57 . 1 1843 ATOM C CG LYS D 274 . −3.091 −9.006 49.920 1.00 25.63 . 1 1844 ATOM C CD LYS D 274 . −3.830 −8.828 51.231 1.00 27.68 . 1 1845 ATOM C CE LYS D 274 . −2.848 −8.611 52.369 1.00 30.93 . 1 1846 ATOM N NZ LYS D 274 . −1.794 −9.665 52.365 1.00 31.10 . 1 1847 ATOM N N ALA D 275 . −1.148 −10.262 47.288 1.00 22.14 . 1 1848 ATOM C CA ALA D 275 . −0.098 −11.258 47.393 1.00 25.16 . 1 1849 ATOM C C ALA D 275 . −0.374 −12.441 46.467 1.00 26.34 . 1 1850 ATOM O O ALA D 275 . −0.172 −13.603 46.834 1.00 25.90 . 1 1851 ATOM C CB ALA D 275 . 0.030 −11.732 48.850 1.00 24.21 . 1 1852 ATOM N N VAL D 276 . −0.856 −12.132 45.266 1.00 26.58 . 1 1853 ATOM C CA VAL D 276 . −1.121 −13.159 44.267 1.00 26.91 . 1 1854 ATOM C C VAL D 276 . −0.086 −13.015 43.150 1.00 26.93 . 1 1855 ATOM O O VAL D 276 . 0.655 −13.952 42.842 1.00 27.53 . 1 1856 ATOM C CB VAL D 276 . −2.546 −13.022 43.671 1.00 26.81 . 1 1857 ATOM C CG1 VAL D 276 . −2.722 −14.007 42.499 1.00 25.93 . 1 1858 ATOM C CG2 VAL D 276 . −3.587 −13.296 44.746 1.00 24.88 . 1 1859 ATOM N N CYS D 277 . −0.025 −11.827 42.559 1.00 27.55 . 1 1860 ATOM C CA CYS D 277 . 0.913 −11.553 41.477 1.00 28.49 . 1 1861 ATOM C C CYS D 277 . 2.368 −11.890 41.804 1.00 30.91 . 1 1862 ATOM O O CYS D 277 . 3.078 −12.450 40.966 1.00 29.27 . 1 1863 ATOM C CB CYS D 277 . 0.842 −10.076 41.071 1.00 29.85 . 1 1864 ATOM S SG CYS D 277 . −0.695 −9.587 40.257 1.00 34.78 . 1 1865 ATOM N N HIS D 278 . 2.818 −11.551 43.013 1.00 30.02 . 1 1866 ATOM C CA HIS D 278 . 4.209 −11.821 43.360 1.00 31.15 . 1 1867 ATOM C C HIS D 278 . 4.579 −13.306 43.347 1.00 31.13 . 1 1868 ATOM O O HIS D 278 . 5.741 −13.663 43.549 1.00 32.23 . 1 1869 ATOM C CB HIS D 278 . 4.584 −11.167 44.705 1.00 30.96 . 1 1870 ATOM C CG HIS D 278 . 4.092 −11.900 45.916 1.00 32.06 . 1 1871 ATOM N ND1 HIS D 278 . 4.617 −11.682 47.173 1.00 31.99 . 1 1872 ATOM C CD2 HIS D 278 . 3.127 −12.838 46.071 1.00 31.66 . 1 1873 ATOM C CE1 HIS D 278 . 3.999 −12.453 48.048 1.00 31.49 . 1 1874 ATOM N NE2 HIS D 278 . 3.090 −13.164 47.405 1.00 31.35 . 1 1875 ATOM N N ASN D 279 . 3.601 −14.169 43.078 1.00 30.51 . 1 1876 ATOM C CA ASN D 279 . 3.852 −15.612 43.018 1.00 31.07 . 1 1877 ATOM C C ASN D 279 . 4.054 −16.094 41.586 1.00 31.92 . 1 1878 ATOM O O ASN D 279 . 4.432 −17.246 41.370 1.00 31.38 . 1 1879 ATOM C CB ASN D 279 . 2.675 −16.405 43.589 1.00 32.70 . 1 1880 ATOM C CG ASN D 279 . 2.529 −16.245 45.076 1.00 32.41 . 1 1881 ATOM O OD1 ASN D 279 . 3.473 −16.471 45.820 1.00 34.26 . 1 1882 ATOM N ND2 ASN D 279 . 1.336 −15.867 45.521 1.00 33.26 . 1 1883 ATOM N N TRP D 280 . 3.812 −15.215 40.618 1.00 30.52 . 1 1884 ATOM C CA TRP D 280 . 3.897 −15.599 39.211 1.00 32.72 . 1 1885 ATOM C C TRP D 280 . 4.776 −14.771 38.283 1.00 32.95 . 1 1886 ATOM O O TRP D 280 . 5.134 −13.634 38.579 1.00 33.86 . 1 1887 ATOM C CB TRP D 280 . 2.484 −15.633 38.628 1.00 31.11 . 1 1888 ATOM C CG TRP D 280 . 1.532 −16.440 39.443 1.00 29.03 . 1 1889 ATOM C CD1 TRP D 280 . 0.711 −15.992 40.436 1.00 28.03 . 1 1890 ATOM C CD2 TRP D 280 . 1.325 −17.851 39.356 1.00 30.56 . 1 1891 ATOM N NE1 TRP D 280 . 0.005 −17.039 40.973 1.00 28.24 . 1 1892 ATOM C CE2 TRP D 280 . 0.363 −18.193 40.329 1.00 29.24 . 1 1893 ATOM C CE3 TRP D 280 . 1.860 −18.862 38.547 1.00 30.24 . 1 1894 ATOM C CZ2 TRP D 280 . −0.076 −19.505 40.517 1.00 31.82 . 1 1895 ATOM C CZ3 TRP D 280 . 1.425 −20.164 38.733 1.00 32.30 . 1 1896 ATOM C CH2 TRP D 280 . 0.466 −20.475 39.710 1.00 32.09 . 1 1897 ATOM N N SER D 281 . 5.105 −15.369 37.140 1.00 35.21 . 1 1898 ATOM C CA SER D 281 . 5.912 −14.720 36.116 1.00 36.16 . 1 1899 ATOM C C SER D 281 . 5.033 −13.688 35.402 1.00 37.51 . 1 1900 ATOM O O SER D 281 . 3.813 −13.657 35.595 1.00 35.96 . 1 1901 ATOM C CB SER D 281 . 6.411 −15.760 35.105 1.00 36.62 . 1 1902 ATOM O OG SER D 281 . 5.321 −16.360 34.417 1.00 39.22 . 1 1903 ATOM N N ASP D 282 . 5.651 −12.842 34.584 1.00 38.45 . 1 1904 ATOM C CA ASP D 282 . 4.907 −11.820 33.853 1.00 40.48 . 1 1905 ATOM C C ASP D 282 . 3.804 −12.442 32.994 1.00 40.04 . 1 1906 ATOM O O ASP D 282 . 2.649 −12.009 33.043 1.00 39.25 . 1 1907 ATOM C CB ASP D 282 . 5.856 −11.004 32.967 1.00 41.86 . 1 1908 ATOM C CG ASP D 282 . 6.686 −10.000 33.759 1.00 45.09 . 1 1909 ATOM O OD1 ASP D 282 . 6.704 −10.081 35.005 1.00 44.26 . 1 1910 ATOM O OD2 ASP D 282 . 7.328 −9.129 33.130 1.00 45.10 . 1 1911 ATOM N N GLU D 283 . 4.162 −13.465 32.221 1.00 41.29 . 1 1912 ATOM C CA GLU D 283 . 3.205 −14.139 31.343 1.00 41.89 . 1 1913 ATOM C C GLU D 283 . 1.965 −14.625 32.076 1.00 40.84 . 1 1914 ATOM O O GLU D 283 . 0.840 −14.339 31.666 1.00 38.53 . 1 1915 ATOM C CB GLU D 283 . 3.865 −15.326 30.638 1.00 46.05 . 1 1916 ATOM C CG GLU D 283 . 4.745 −14.944 29.466 1.00 51.61 . 1 1917 ATOM C CD GLU D 283 . 5.310 −16.158 28.749 1.00 56.15 . 1 1918 ATOM O OE1 GLU D 283 . 4.540 −17.119 28.509 1.00 57.16 . 1 1919 ATOM O OE2 GLU D 283 . 6.518 −16.148 28.421 1.00 57.74 . 1 1920 ATOM N N LYS D 284 . 2.174 −15.366 33.159 1.00 38.38 . 1 1921 ATOM C CA LYS D 284 . 1.064 −15.892 33.931 1.00 38.66 . 1 1922 ATOM C C LYS D 284 . 0.222 −14.779 34.552 1.00 37.67 . 1 1923 ATOM O O LYS D 284 . −1.006 −14.871 34.568 1.00 39.27 . 1 1924 ATOM C CB LYS D 284 . 1.594 −16.859 34.990 1.00 40.93 . 1 1925 ATOM C CG LYS D 284 . 2.322 −18.043 34.359 1.00 45.53 . 1 1926 ATOM C CD LYS D 284 . 2.968 −18.953 35.389 1.00 50.57 . 1 1927 ATOM C CE LYS D 284 . 3.672 −20.133 34.716 1.00 53.34 . 1 1928 ATOM N NZ LYS D 284 . 4.305 −21.058 35.705 1.00 54.80 . 1 1929 ATOM N N CYS D 285 . 0.864 −13.722 35.046 1.00 36.56 . 1 1930 ATOM C CA CYS D 285 . 0.113 −12.607 35.624 1.00 35.47 . 1 1931 ATOM C C CYS D 285 . −0.814 −12.013 34.562 1.00 36.30 . 1 1932 ATOM O O CYS D 285 . −1.987 −11.728 34.823 1.00 34.14 . 1 1933 ATOM C CB CYS D 285 . 1.056 −11.518 36.131 1.00 36.12 . 1 1934 ATOM S SG CYS D 285 . 1.872 −11.912 37.704 1.00 34.62 . 1 1935 ATOM N N ILE D 286 . −0.273 −11.821 33.363 1.00 36.16 . 1 1936 ATOM C CA ILE D 286 . −1.050 −11.265 32.264 1.00 37.16 . 1 1937 ATOM C C ILE D 286 . −2.250 −12.168 31.977 1.00 36.65 . 1 1938 ATOM O O ILE D 286 . −3.329 −11.689 31.644 1.00 37.12 . 1 1939 ATOM C CB ILE D 286 . −0.176 −11.115 30.998 1.00 38.50 . 1 1940 ATOM C CG1 ILE D 286 . 0.952 −10.115 31.275 1.00 37.82 . 1 1941 ATOM C CG2 ILE D 286 . −1.026 −10.639 29.821 1.00 37.02 . 1 1942 ATOM C CD1 ILE D 286 . 2.012 −10.057 30.200 1.00 37.85 . 1 1943 ATOM N N GLU D 287 . −2.066 −13.474 32.127 1.00 38.48 . 1 1944 ATOM C CA GLU D 287 . −3.156 −14.405 31.891 1.00 39.92 . 1 1945 ATOM C C GLU D 287 . −4.346 −14.211 32.823 1.00 40.24 . 1 1946 ATOM O O GLU D 287 . −5.463 −13.981 32.352 1.00 38.12 . 1 1947 ATOM C CB GLU D 287 . −2.667 −15.846 31.997 1.00 44.04 . 1 1948 ATOM C CG GLU D 287 . −1.940 −16.339 30.762 1.00 49.60 . 1 1949 ATOM C CD GLU D 287 . −1.721 −17.833 30.796 1.00 52.45 . 1 1950 ATOM O OE1 GLU D 287 . −2.701 −18.556 31.078 1.00 54.32 . 1 1951 ATOM O OE2 GLU D 287 . −0.582 −18.283 30.538 1.00 53.77 . 1 1952 ATOM N N PHE D 288 . −4.134 −14.307 34.137 1.00 37.99 . 1 1953 ATOM C CA PHE D 288 . −5.263 −14.134 35.044 1.00 36.60 . 1 1954 ATOM C C PHE D 288 . −5.721 −12.684 35.158 1.00 36.29 . 1 1955 ATOM O O PHE D 288 . −6.894 −12.422 35.424 1.00 37.68 . 1 1956 ATOM C CB PHE D 288 . −4.995 −14.768 36.432 1.00 35.24 . 1 1957 ATOM C CG PHE D 288 . −3.763 −14.261 37.141 1.00 33.80 . 1 1958 ATOM C CD1 PHE D 288 . −3.733 −12.990 37.709 1.00 34.85 . 1 1959 ATOM C CD2 PHE D 288 . −2.662 −15.093 37.315 1.00 35.29 . 1 1960 ATOM C CE1 PHE D 288 . −2.621 −12.555 38.451 1.00 34.78 . 1 1961 ATOM C CE2 PHE D 288 . −1.545 −14.671 38.052 1.00 35.22 . 1 1962 ATOM C CZ PHE D 288 . −1.527 −13.400 38.622 1.00 32.32 . 1 1963 ATOM N N LEU D 289 . −4.816 −11.739 34.936 1.00 35.67 . 1 1964 ATOM C CA LEU D 289 . −5.204 −10.334 34.984 1.00 37.13 . 1 1965 ATOM C C LEU D 289 . −6.129 −10.057 33.795 1.00 38.17 . 1 1966 ATOM O O LEU D 289 . −7.087 −9.289 33.903 1.00 38.68 . 1 1967 ATOM C CB LEU D 289 . −3.972 −9.426 34.925 1.00 36.70 . 1 1968 ATOM C CG LEU D 289 . −3.152 −9.331 36.223 1.00 36.52 . 1 1969 ATOM C CD1 LEU D 289 . −1.838 −8.598 35.966 1.00 36.24 . 1 1970 ATOM C CD2 LEU D 289 . −3.969 −8.610 37.292 1.00 35.46 . 1 1971 ATOM N N SER D 290 . −5.837 −10.690 32.662 1.00 38.53 . 1 1972 ATOM C CA SER D 290 . −6.666 −10.528 31.472 1.00 40.18 . 1 1973 ATOM C C SER D 290 . −8.033 −11.152 31.742 1.00 39.13 . 1 1974 ATOM O O SER D 290 . −9.062 −10.632 31.306 1.00 40.36 . 1 1975 ATOM C CB SER D 290 . −6.003 −11.193 30.261 1.00 38.59 . 1 1976 ATOM O OG SER D 290 . −4.862 −10.461 29.844 1.00 39.15 . 1 1977 ATOM N N ASN D 291 . −8.044 −12.265 32.472 1.00 39.82 . 1 1978 ATOM C CA ASN D 291 . −9.300 −12.919 32.808 1.00 39.54 . 1 1979 ATOM C C ASN D 291 . −10.092 −12.025 33.757 1.00 39.47 . 1 1980 ATOM O O ASN D 291 . −11.323 −12.003 33.724 1.00 40.30 . 1 1981 ATOM C CB ASN D 291 . −9.058 −14.295 33.440 1.00 40.28 . 1 1982 ATOM C CG ASN D 291 . −8.660 −15.346 32.416 1.00 43.65 . 1 1983 ATOM O OD1 ASN D 291 . −9.066 −15.275 31.254 1.00 44.66 . 1 1984 ATOM N ND2 ASN D 291 . −7.882 −16.339 32.844 1.00 43.17 . 1 1985 ATOM N N CYS D 292 . −9.388 −11.283 34.605 1.00 39.08 . 1 1986 ATOM C CA CYS D 292 . −10.056 −10.373 35.526 1.00 38.36 . 1 1987 ATOM C C CYS D 292 . −10.708 −9.262 34.708 1.00 40.29 . 1 1988 ATOM O O CYS D 292 . −11.861 −8.894 34.938 1.00 39.55 . 1 1989 ATOM C CB CYS D 292 . −9.053 −9.749 36.504 1.00 37.55 . 1 1990 ATOM S SG CYS D 292 . −8.434 −10.874 37.771 1.00 36.71 . 1 1991 ATOM N N HIS D 293 . −9.956 −8.740 33.743 1.00 41.26 . 1 1992 ATOM C CA HIS D 293 . −10.435 −7.656 32.896 1.00 43.00 . 1 1993 ATOM C C HIS D 293 . −11.745 −7.960 32.170 1.00 43.53 . 1 1994 ATOM O O HIS D 293 . −12.659 −7.136 32.162 1.00 43.81 . 1 1995 ATOM C CB HIS D 293 . −9.353 −7.281 31.881 1.00 44.43 . 1 1996 ATOM C CG HIS D 293 . −9.654 −6.034 31.109 1.00 46.01 . 1 1997 ATOM N ND1 HIS D 293 . −10.584 −5.992 30.092 1.00 46.70 . 1 1998 ATOM C CD2 HIS D 293 . −9.164 −4.776 31.222 1.00 46.16 . 1 1999 ATOM C CE1 HIS D 293 . −10.653 −4.763 29.612 1.00 45.79 . 1 2000 ATOM N NE2 HIS D 293 . −9.802 −4.006 30.281 1.00 46.74 . 1 2001 ATOM N N LYS D 294 . −11.846 −9.142 31.574 1.00 44.25 . 1 2002 ATOM C CA LYS D 294 . −13.051 −9.492 30.837 1.00 46.28 . 1 2003 ATOM C C LYS D 294 . −14.240 −9.815 31.726 1.00 46.42 . 1 2004 ATOM O O LYS D 294 . −15.380 −9.812 31.262 1.00 46.59 . 1 2005 ATOM C CB LYS D 294 . −12.781 −10.662 29.887 1.00 48.70 . 1 2006 ATOM C CG LYS D 294 . −12.483 −11.982 30.556 1.00 51.01 . 1 2007 ATOM C CD LYS D 294 . −12.194 −13.042 29.502 1.00 55.15 . 1 2008 ATOM C CE LYS D 294 . −11.804 −14.372 30.129 1.00 57.43 . 1 2009 ATOM N NZ LYS D 294 . −11.376 −15.361 29.096 1.00 59.23 . 1 2010 ATOM N N ALA D 295 . −13.984 −10.090 33.001 1.00 44.50 . 1 2011 ATOM C CA ALA D 295 . −15.066 −10.404 33.924 1.00 43.21 . 1 2012 ATOM C C ALA D 295 . −15.465 −9.157 34.715 1.00 42.29 . 1 2013 ATOM O O ALA D 295 . −16.441 −9.166 35.463 1.00 42.23 . 1 2014 ATOM C CB ALA D 295 . −14.640 −11.526 34.871 1.00 42.36 . 1 2015 ATOM N N LEU D 296 . −14.706 −8.082 34.535 1.00 41.98 . 1 2016 ATOM C CA LEU D 296 . −14.973 −6.827 35.232 1.00 44.91 . 1 2017 ATOM C C LEU D 296 . −16.103 −6.023 34.604 1.00 47.08 . 1 2018 ATOM O O LEU D 296 . −16.305 −6.061 33.393 1.00 47.87 . 1 2019 ATOM C CB LEU D 296 . −13.729 −5.943 35.241 1.00 44.33 . 1 2020 ATOM C CG LEU D 296 . −12.823 −5.908 36.469 1.00 44.40 . 1 2021 ATOM C CD1 LEU D 296 . −11.755 −4.856 36.235 1.00 43.55 . 1 2022 ATOM C CD2 LEU D 296 . −13.628 −5.579 37.718 1.00 43.18 . 1 2023 ATOM N N SER D 297 . −16.825 −5.282 35.435 1.00 48.23 . 1 2024 ATOM C CA SER D 297 . −17.899 −4.443 34.941 1.00 50.36 . 1 2025 ATOM C C SER D 297 . −17.251 −3.324 34.125 1.00 51.63 . 1 2026 ATOM O O SER D 297 . −16.069 −3.017 34.305 1.00 51.70 . 1 2027 ATOM C CB SER D 297 . −18.692 −3.856 36.108 1.00 51.42 . 1 2028 ATOM O OG SER D 297 . −19.326 −4.888 36.842 1.00 56.27 . 1 2029 ATOM N N PRO D 298 . −18.017 −2.703 33.215 1.00 51.86 . 1 2030 ATOM C CA PRO D 298 . −17.528 −1.617 32.361 1.00 51.73 . 1 2031 ATOM C C PRO D 298 . −16.662 −0.554 33.044 1.00 50.94 . 1 2032 ATOM O O PRO D 298 . −15.583 −0.221 32.554 1.00 52.87 . 1 2033 ATOM C CB PRO D 298 . −18.819 −1.041 31.783 1.00 51.87 . 1 2034 ATOM C CG PRO D 298 . −19.653 −2.280 31.606 1.00 52.14 . 1 2035 ATOM C CD PRO D 298 . −19.431 −3.004 32.919 1.00 52.10 . 1 2036 ATOM N N ASN D 299 . −17.124 −0.027 34.172 1.00 49.68 . 1 2037 ATOM C CA ASN D 299 . −16.377 1.012 34.876 1.00 48.69 . 1 2038 ATOM C C ASN D 299 . −15.654 0.495 36.125 1.00 47.33 . 1 2039 ATOM O O ASN D 299 . −15.396 1.255 37.062 1.00 45.06 . 1 2040 ATOM C CB ASN D 299 . −17.334 2.143 35.260 1.00 50.59 . 1 2041 ATOM C CG ASN D 299 . −18.056 2.727 34.057 1.00 52.99 . 1 2042 ATOM O OD1 ASN D 299 . −19.033 3.465 34.200 1.00 55.10 . 1 2043 ATOM N ND2 ASN D 299 . −17.572 2.402 32.862 1.00 53.11 . 1 2044 ATOM N N GLY D 300 . −15.318 −0.792 36.124 1.00 45.13 . 1 2045 ATOM C CA GLY D 300 . −14.651 −1.388 37.271 1.00 42.51 . 1 2046 ATOM C C GLY D 300 . −13.141 −1.240 37.335 1.00 41.01 . 1 2047 ATOM O O GLY D 300 . −12.517 −0.582 36.499 1.00 40.15 . 1 2048 ATOM N N LYS D 301 . −12.550 −1.869 38.346 1.00 38.99 . 1 2049 ATOM C CA LYS D 301 . −11.110 −1.817 38.541 1.00 37.94 . 1 2050 ATOM C C LYS D 301 . −10.613 −3.039 39.297 1.00 37.89 . 1 2051 ATOM O O LYS D 301 . −11.388 −3.747 39.951 1.00 36.40 . 1 2052 ATOM C CB LYS D 301 . −10.737 −0.578 39.349 1.00 37.28 . 1 2053 ATOM C CG LYS D 301 . −11.293 −0.615 40.758 1.00 36.51 . 1 2054 ATOM C CD LYS D 301 . −10.999 0.657 41.525 1.00 34.92 . 1 2055 ATOM C CE LYS D 301 . −11.755 0.666 42.837 1.00 34.59 . 1 2056 ATOM N NZ LYS D 301 . −11.601 1.958 43.561 1.00 34.49 . 1 2057 ATOM N N VAL D 302 . −9.311 −3.274 39.189 1.00 37.88 . 1 2058 ATOM C CA VAL D 302 . −8.654 −4.365 39.888 1.00 37.01 . 1 2059 ATOM C C VAL D 302 . −7.748 −3.695 40.910 1.00 37.78 . 1 2060 ATOM O O VAL D 302 . −7.053 −2.722 40.591 1.00 36.77 . 1 2061 ATOM C CB VAL D 302 . −7.797 −5.228 38.938 1.00 37.26 . 1 2062 ATOM C CG1 VAL D 302 . −6.706 −5.944 39.725 1.00 39.86 . 1 2063 ATOM C CG2 VAL D 302 . −8.678 −6.254 38.242 1.00 37.84 . 1 2064 ATOM N N ILE D 303 . −7.778 −4.208 42.138 1.00 34.07 . 1 2065 ATOM C CA ILE D 303 . −6.972 −3.671 43.221 1.00 33.53 . 1 2066 ATOM C C ILE D 303 . −5.843 −4.650 43.528 1.00 32.38 . 1 2067 ATOM O O ILE D 303 . −6.089 −5.795 43.902 1.00 33.03 . 1 2068 ATOM C CB ILE D 303 . −7.822 −3.472 44.492 1.00 34.89 . 1 2069 ATOM C CG1 ILE D 303 . −9.096 −2.697 44.149 1.00 33.98 . 1 2070 ATOM C CG2 ILE D 303 . −7.018 −2.724 45.543 1.00 35.58 . 1 2071 ATOM C CD1 ILE D 303 . −10.023 −2.496 45.322 1.00 34.80 . 1 2072 ATOM N N ILE D 304 . −4.609 −4.191 43.365 1.00 31.35 . 1 2073 ATOM C CA ILE D 304 . −3.437 −5.018 43.617 1.00 31.86 . 1 2074 ATOM C C ILE D 304 . −2.766 −4.566 44.906 1.00 32.71 . 1 2075 ATOM O O ILE D 304 . −2.418 −3.395 45.053 1.00 32.38 . 1 2076 ATOM C CB ILE D 304 . −2.421 −4.911 42.458 1.00 33.03 . 1 2077 ATOM C CG1 ILE D 304 . −3.102 −5.273 41.135 1.00 33.04 . 1 2078 ATOM C CG2 ILE D 304 . −1.243 −5.841 42.699 1.00 31.75 . 1 2079 ATOM C CD1 ILE D 304 . −3.600 −6.700 41.058 1.00 33.07 . 1 2080 ATOM N N VAL D 305 . −2.608 −5.494 45.847 1.00 31.35 . 1 2081 ATOM C CA VAL D 305 . −1.968 −5.180 47.114 1.00 29.88 . 1 2082 ATOM C C VAL D 305 . −0.679 −5.980 47.182 1.00 29.21 . 1 2083 ATOM O O VAL D 305 . −0.685 −7.180 47.475 1.00 26.96 . 1 2084 ATOM C CB VAL D 305 . −2.874 −5.536 48.308 1.00 31.03 . 1 2085 ATOM C CG1 VAL D 305 . −2.227 −5.075 49.606 1.00 28.30 . 1 2086 ATOM C CG2 VAL D 305 . −4.234 −4.875 48.145 1.00 31.05 . 1 2087 ATOM N N GLU D 306 . 0.424 −5.299 46.888 1.00 27.22 . 1 2088 ATOM C CA GLU D 306 . 1.745 −5.907 46.872 1.00 27.66 . 1 2089 ATOM C C GLU D 306 . 2.769 −4.866 47.294 1.00 28.06 . 1 2090 ATOM O O GLU D 306 . 2.522 −3.670 47.189 1.00 27.14 . 1 2091 ATOM C CB GLU D 306 . 2.096 −6.376 45.453 1.00 27.20 . 1 2092 ATOM C CG GLU D 306 . 1.169 −7.433 44.860 1.00 28.75 . 1 2093 ATOM C CD GLU D 306 . 1.563 −8.845 45.255 1.00 31.00 . 1 2094 ATOM O OE1 GLU D 306 . 2.364 −8.995 46.204 1.00 29.08 . 1 2095 ATOM O OE2 GLU D 306 . 1.072 −9.805 44.623 1.00 31.75 . 1 2096 ATOM N N PHE D 307 . 3.918 −5.311 47.788 1.00 29.72 . 1 2097 ATOM C CA PHE D 307 . 4.950 −4.359 48.147 1.00 28.74 . 1 2098 ATOM C C PHE D 307 . 5.539 −3.805 46.852 1.00 30.74 . 1 2099 ATOM O O PHE D 307 . 5.548 −4.476 45.818 1.00 28.59 . 1 2100 ATOM C CB PHE D 307 . 6.049 −5.022 48.974 1.00 30.48 . 1 2101 ATOM C CG PHE D 307 . 5.672 −5.226 50.410 1.00 27.59 . 1 2102 ATOM C CD1 PHE D 307 . 5.034 −6.390 50.817 1.00 27.49 . 1 2103 ATOM C CD2 PHE D 307 . 5.913 −4.224 51.348 1.00 27.88 . 1 2104 ATOM C CE1 PHE D 307 . 4.636 −6.561 52.134 1.00 27.11 . 1 2105 ATOM C CE2 PHE D 307 . 5.518 −4.381 52.675 1.00 27.82 . 1 2106 ATOM C CZ PHE D 307 . 4.877 −5.553 53.071 1.00 28.50 . 1 2107 ATOM N N ILE D 308 . 6.034 −2.577 46.902 1.00 30.63 . 1 2108 ATOM C CA ILE D 308 . 6.605 −1.990 45.703 1.00 31.13 . 1 2109 ATOM C C ILE D 308 . 8.117 −1.848 45.800 1.00 30.86 . 1 2110 ATOM O O ILE D 308 . 8.625 −1.095 46.633 1.00 30.41 . 1 2111 ATOM C CB ILE D 308 . 5.969 −0.616 45.413 1.00 31.75 . 1 2112 ATOM C CG1 ILE D 308 . 4.465 −0.796 45.162 1.00 32.26 . 1 2113 ATOM C CG2 ILE D 308 . 6.638 0.029 44.198 1.00 32.02 . 1 2114 ATOM C CD1 ILE D 308 . 3.700 0.503 44.976 1.00 32.08 . 1 2115 ATOM N N LEU D 309 . 8.822 −2.594 44.953 1.00 30.30 . 1 2116 ATOM C CA LEU D 309 . 10.274 −2.550 44.889 1.00 32.86 . 1 2117 ATOM C C LEU D 309 . 10.671 −1.185 44.349 1.00 34.63 . 1 2118 ATOM O O LEU D 309 . 10.109 −0.721 43.355 1.00 34.29 . 1 2119 ATOM C CB LEU D 309 . 10.811 −3.605 43.917 1.00 33.17 . 1 2120 ATOM C CG LEU D 309 . 11.528 −4.882 44.367 1.00 36.81 . 1 2121 ATOM C CD1 LEU D 309 . 12.151 −5.528 43.127 1.00 35.36 . 1 2122 ATOM C CD2 LEU D 309 . 12.615 −4.584 45.389 1.00 33.52 . 1 2123 ATOM N N PRO D 310 . 11.648 −0.525 44.987 1.00 35.16 . 1 2124 ATOM C CA PRO D 310 . 12.093 0.796 44.519 1.00 34.64 . 1 2125 ATOM C C PRO D 310 . 12.630 0.673 43.094 1.00 34.16 . 1 2126 ATOM O O PRO D 310 . 13.241 −0.338 42.743 1.00 32.63 . 1 2127 ATOM C CB PRO D 310 . 13.191 1.164 45.513 1.00 34.50 . 1 2128 ATOM C CG PRO D 310 . 12.754 0.453 46.777 1.00 35.44 . 1 2129 ATOM C CD PRO D 310 . 12.312 −0.891 46.252 1.00 35.41 . 1 2130 ATOM N N GLU D 311 . 12.397 1.696 42.275 1.00 35.82 . 1 2131 ATOM C CA GLU D 311 . 12.866 1.693 40.890 1.00 34.27 . 1 2132 ATOM C C GLU D 311 . 14.333 1.297 40.884 1.00 32.73 . 1 2133 ATOM O O GLU D 311 . 14.762 0.427 40.121 1.00 30.82 . 1 2134 ATOM C CB GLU D 311 . 12.692 3.085 40.275 1.00 35.98 . 1 2135 ATOM C CG GLU D 311 . 13.202 3.219 38.854 1.00 39.55 . 1 2136 ATOM C CD GLU D 311 . 12.585 2.207 37.908 1.00 41.43 . 1 2137 ATOM O OE1 GLU D 311 . 11.433 1.780 38.150 1.00 40.05 . 1 2138 ATOM O OE2 GLU D 311 . 13.253 1.852 36.911 1.00 42.00 . 1 2139 ATOM N N GLU D 312 . 15.099 1.955 41.743 1.00 33.18 . 1 2140 ATOM C CA GLU D 312 . 16.514 1.663 41.886 1.00 33.63 . 1 2141 ATOM C C GLU D 312 . 16.746 1.331 43.357 1.00 32.11 . 1 2142 ATOM O O GLU D 312 . 16.110 1.908 44.240 1.00 31.56 . 1 2143 ATOM C CB GLU D 312 . 17.359 2.877 41.489 1.00 36.80 . 1 2144 ATOM C CG GLU D 312 . 17.326 3.214 40.004 1.00 36.43 . 1 2145 ATOM C CD GLU D 312 . 17.806 2.071 39.144 1.00 38.08 . 1 2146 ATOM O OE1 GLU D 312 . 18.785 1.402 39.538 1.00 39.68 . 1 2147 ATOM O OE2 GLU D 312 . 17.215 1.843 38.066 1.00 39.34 . 1 2148 ATOM N N PRO D 313 . 17.643 0.379 43.640 1.00 32.67 . 1 2149 ATOM C CA PRO D 313 . 17.895 0.034 45.041 1.00 33.10 . 1 2150 ATOM C C PRO D 313 . 18.595 1.166 45.792 1.00 33.38 . 1 2151 ATOM O O PRO D 313 . 19.409 1.890 45.220 1.00 31.90 . 1 2152 ATOM C CB PRO D 313 . 18.761 −1.219 44.929 1.00 32.91 . 1 2153 ATOM C CG PRO D 313 . 19.500 −1.001 43.636 1.00 32.09 . 1 2154 ATOM C CD PRO D 313 . 18.393 −0.511 42.738 1.00 31.49 . 1 2155 ATOM N N ASN D 314 . 18.255 1.326 47.066 1.00 33.21 . 1 2156 ATOM C CA ASN D 314 . 18.877 2.345 47.899 1.00 34.71 . 1 2157 ATOM C C ASN D 314 . 19.006 1.828 49.328 1.00 33.51 . 1 2158 ATOM O O ASN D 314 . 18.604 0.706 49.619 1.00 32.58 . 1 2159 ATOM C CB ASN D 314 . 18.091 3.670 47.846 1.00 34.40 . 1 2160 ATOM C CG ASN D 314 . 16.629 3.513 48.211 1.00 35.34 . 1 2161 ATOM O OD1 ASN D 314 . 15.746 3.873 47.433 1.00 37.19 . 1 2162 ATOM N ND2 ASN D 314 . 16.364 2.994 49.399 1.00 32.57 . 1 2163 ATOM N N THR D 315 . 19.567 2.636 50.220 1.00 33.82 . 1 2164 ATOM C CA THR D 315 . 19.767 2.196 51.599 1.00 32.65 . 1 2165 ATOM C C THR D 315 . 18.579 2.398 52.540 1.00 33.69 . 1 2166 ATOM O O THR D 315 . 18.719 2.241 53.752 1.00 34.60 . 1 2167 ATOM C CB THR D 315 . 21.007 2.887 52.224 1.00 32.51 . 1 2168 ATOM O OG1 THR D 315 . 20.831 4.309 52.198 1.00 32.85 . 1 2169 ATOM C CG2 THR D 315 . 22.262 2.532 51.447 1.00 30.92 . 1 2170 ATOM N N SER D 316 . 17.409 2.731 52.001 1.00 31.90 . 1 2171 ATOM C CA SER D 316 . 16.246 2.945 52.856 1.00 30.53 . 1 2172 ATOM C C SER D 316 . 15.669 1.635 53.394 1.00 29.75 . 1 2173 ATOM O O SER D 316 . 15.987 0.557 52.906 1.00 27.85 . 1 2174 ATOM C CB SER D 316 . 15.142 3.685 52.105 1.00 30.29 . 1 2175 ATOM O OG SER D 316 . 14.493 2.828 51.187 1.00 30.64 . 1 2176 ATOM N N GLU D 317 . 14.817 1.770 54.404 1.00 30.35 . 1 2177 ATOM C CA GLU D 317 . 14.138 0.657 55.056 1.00 33.74 . 1 2178 ATOM C C GLU D 317 . 13.268 −0.087 54.040 1.00 31.69 . 1 2179 ATOM O O GLU D 317 . 13.261 −1.320 53.993 1.00 30.02 . 1 2180 ATOM C CB GLU D 317 . 13.234 1.201 56.165 1.00 35.55 . 1 2181 ATOM C CG GLU D 317 . 13.214 0.406 57.446 1.00 44.55 . 1 2182 ATOM C CD GLU D 317 . 14.420 0.694 58.303 1.00 44.94 . 1 2183 ATOM O OE1 GLU D 317 . 14.428 0.283 59.482 1.00 46.11 . 1 2184 ATOM O OE2 GLU D 317 . 15.361 1.331 57.786 1.00 48.23 . 1 2185 ATOM N N GLU D 318 . 12.519 0.667 53.238 1.00 30.65 . 1 2186 ATOM C CA GLU D 318 . 11.646 0.043 52.247 1.00 30.98 . 1 2187 ATOM C C GLU D 318 . 12.447 −0.749 51.232 1.00 29.41 . 1 2188 ATOM O O GLU D 318 . 12.013 −1.818 50.802 1.00 28.52 . 1 2189 ATOM C CB GLU D 318 . 10.782 1.086 51.522 1.00 35.93 . 1 2190 ATOM C CG GLU D 318 . 11.560 2.190 50.855 1.00 37.57 . 1 2191 ATOM C CD GLU D 318 . 11.532 3.477 51.656 1.00 41.50 . 1 2192 ATOM O OE1 GLU D 318 . 11.616 3.408 52.905 1.00 38.92 . 1 2193 ATOM O OE2 GLU D 318 . 11.431 4.557 51.028 1.00 40.93 . 1 2194 ATOM N N SER D 319 . 13.610 −0.235 50.838 1.00 27.49 . 1 2195 ATOM C CA SER D 319 . 14.432 −0.960 49.879 1.00 27.13 . 1 2196 ATOM C C SER D 319 . 14.941 −2.250 50.545 1.00 27.06 . 1 2197 ATOM O O SER D 319 . 14.933 −3.327 49.941 1.00 25.01 . 1 2198 ATOM C CB SER D 319 . 15.604 −0.091 49.401 1.00 25.17 . 1 2199 ATOM O OG SER D 319 . 16.309 −0.723 48.345 1.00 25.30 . 1 2200 ATOM N N LYS D 320 . 15.381 −2.141 51.795 1.00 27.10 . 1 2201 ATOM C CA LYS D 320 . 15.852 −3.315 52.520 1.00 28.16 . 1 2202 ATOM C C LYS D 320 . 14.737 −4.355 52.601 1.00 26.88 . 1 2203 ATOM O O LYS D 320 . 14.960 −5.531 52.321 1.00 25.39 . 1 2204 ATOM C CB LYS D 320 . 16.287 −2.941 53.944 1.00 27.10 . 1 2205 ATOM C CG LYS D 320 . 17.644 −2.254 54.049 1.00 29.15 . 1 2206 ATOM C CD LYS D 320 . 18.018 −2.047 55.522 1.00 30.84 . 1 2207 ATOM C CE LYS D 320 . 19.415 −1.452 55.689 1.00 32.70 . 1 2208 ATOM N NZ LYS D 320 . 19.512 −0.080 55.126 1.00 37.53 . 1 2209 ATOM N N LEU D 321 . 13.530 −3.911 52.952 1.00 28.00 . 1 2210 ATOM C CA LEU D 321 . 12.403 −4.825 53.101 1.00 26.86 . 1 2211 ATOM C C LEU D 321 . 11.929 −5.496 51.825 1.00 28.01 . 1 2212 ATOM O O LEU D 321 . 11.864 −6.720 51.751 1.00 26.01 . 1 2213 ATOM C CB LEU D 321 . 11.200 −4.128 53.751 1.00 26.83 . 1 2214 ATOM C CG LEU D 321 . 9.957 −5.031 53.860 1.00 25.65 . 1 2215 ATOM C CD1 LEU D 321 . 10.267 −6.195 54.819 1.00 26.93 . 1 2216 ATOM C CD2 LEU D 321 . 8.749 −4.248 54.358 1.00 27.71 . 1 2217 ATOM N N VAL D 322 . 11.590 −4.710 50.809 1.00 26.98 . 1 2218 ATOM C CA VAL D 322 . 11.086 −5.329 49.598 1.00 25.27 . 1 2219 ATOM C C VAL D 322 . 12.132 −6.217 48.936 1.00 25.02 . 1 2220 ATOM O O VAL D 322 . 11.797 −7.277 48.410 1.00 27.88 . 1 2221 ATOM C CB VAL D 322 . 10.529 −4.267 48.624 1.00 24.28 . 1 2222 ATOM C CG1 VAL D 322 . 9.785 −4.952 47.473 1.00 24.50 . 1 2223 ATOM C CG2 VAL D 322 . 9.577 −3.352 49.370 1.00 23.89 . 1 2224 ATOM N N SER D 323 . 13.401 −5.815 48.966 1.00 24.96 . 1 2225 ATOM C CA SER D 323 . 14.437 −6.658 48.380 1.00 24.57 . 1 2226 ATOM C C SER D 323 . 14.606 −7.938 49.216 1.00 25.05 . 1 2227 ATOM O O SER D 323 . 14.938 −9.000 48.683 1.00 25.15 . 1 2228 ATOM C CB SER D 323 . 15.774 −5.910 48.279 1.00 26.14 . 1 2229 ATOM O OG SER D 323 . 15.897 −5.256 47.020 1.00 28.19 . 1 2230 ATOM N N THR D 324 . 14.372 −7.843 50.521 1.00 25.30 . 1 2231 ATOM C CA THR D 324 . 14.478 −9.030 51.381 1.00 25.32 . 1 2232 ATOM C C THR D 324 . 13.363 −10.004 51.010 1.00 25.46 . 1 2233 ATOM O O THR D 324 . 13.597 −11.201 50.852 1.00 25.91 . 1 2234 ATOM C CB THR D 324 . 14.347 −8.665 52.870 1.00 25.78 . 1 2235 ATOM O OG1 THR D 324 . 15.565 −8.061 53.313 1.00 22.92 . 1 2236 ATOM C CG2 THR D 324 . 14.075 −9.912 53.718 1.00 24.98 . 1 2237 ATOM N N LEU D 325 . 12.152 −9.478 50.856 1.00 25.52 . 1 2238 ATOM C CA LEU D 325 . 11.006 −10.304 50.486 1.00 26.48 . 1 2239 ATOM C C LEU D 325 . 11.227 −10.883 49.092 1.00 28.92 . 1 2240 ATOM O O LEU D 325 . 10.899 −12.042 48.832 1.00 28.90 . 1 2241 ATOM C CB LEU D 325 . 9.720 −9.469 50.502 1.00 26.54 . 1 2242 ATOM C CG LEU D 325 . 9.295 −8.906 51.863 1.00 29.12 . 1 2243 ATOM C CD1 LEU D 325 . 8.035 −8.069 51.721 1.00 28.75 . 1 2244 ATOM C CD2 LEU D 325 . 9.038 −10.056 52.839 1.00 29.35 . 1 2245 ATOM N N ASP D 326 . 11.780 −10.068 48.197 1.00 29.32 . 1 2246 ATOM C CA ASP D 326 . 12.050 −10.509 46.835 1.00 29.77 . 1 2247 ATOM C C ASP D 326 . 12.950 −11.751 46.856 1.00 30.50 . 1 2248 ATOM O O ASP D 326 . 12.669 −12.742 46.177 1.00 27.68 . 1 2249 ATOM C CB ASP D 326 . 12.701 −9.372 46.039 1.00 31.50 . 1 2250 ATOM C CG ASP D 326 . 12.879 −9.708 44.565 1.00 33.10 . 1 2251 ATOM O OD1 ASP D 326 . 12.036 −10.442 44.011 1.00 34.64 . 1 2252 ATOM O OD2 ASP D 326 . 13.855 −9.220 43.957 1.00 34.74 . 1 2253 ATOM N N ASN D 327 . 14.018 −11.709 47.649 1.00 27.65 . 1 2254 ATOM C CA ASN D 327 . 14.926 −12.846 47.743 1.00 30.44 . 1 2255 ATOM C C ASN D 327 . 14.255 −14.015 48.448 1.00 31.38 . 1 2256 ATOM O O ASN D 327 . 14.540 −15.180 48.164 1.00 31.50 . 1 2257 ATOM C CB ASN D 327 . 16.214 −12.439 48.471 1.00 30.34 . 1 2258 ATOM C CG ASN D 327 . 17.201 −11.748 47.548 1.00 32.11 . 1 2259 ATOM O OD1 ASN D 327 . 17.883 −12.400 46.759 1.00 32.50 . 1 2260 ATOM N ND2 ASN D 327 . 17.268 −10.423 47.626 1.00 29.33 . 1 2261 ATOM N N LEU D 328 . 13.355 −13.697 49.368 1.00 30.74 . 1 2262 ATOM C CA LEU D 328 . 12.620 −14.723 50.084 1.00 33.01 . 1 2263 ATOM C C LEU D 328 . 11.676 −15.438 49.109 1.00 33.78 . 1 2264 ATOM O O LEU D 328 . 11.593 −16.663 49.114 1.00 33.40 . 1 2265 ATOM C CB LEU D 328 . 11.819 −14.093 51.222 1.00 32.32 . 1 2266 ATOM C CG LEU D 328 . 10.884 −15.014 52.008 1.00 36.09 . 1 2267 ATOM C CD1 LEU D 328 . 11.682 −16.146 52.636 1.00 35.34 . 1 2268 ATOM C CD2 LEU D 328 . 10.161 −14.207 53.071 1.00 35.94 . 1 2269 ATOM N N MET D 329 . 10.977 −14.668 48.274 1.00 34.98 . 1 2270 ATOM C CA MET D 329 . 10.037 −15.236 47.306 1.00 37.79 . 1 2271 ATOM C C MET D 329 . 10.750 −16.118 46.302 1.00 39.17 . 1 2272 ATOM O O MET D 329 . 10.320 −17.240 46.015 1.00 40.47 . 1 2273 ATOM C CB MET D 329 . 9.288 −14.131 46.551 1.00 36.53 . 1 2274 ATOM C CG MET D 329 . 8.282 −13.369 47.385 1.00 37.83 . 1 2275 ATOM S SD MET D 329 . 7.161 −14.468 48.265 1.00 39.84 . 1 2276 ATOM C CE MET D 329 . 6.157 −15.133 46.899 1.00 38.40 . 1 2277 ATOM N N PHE D 330 . 11.843 −15.601 45.761 1.00 41.21 . 1 2278 ATOM C CA PHE D 330 . 12.625 −16.337 44.786 1.00 44.41 . 1 2279 ATOM C C PHE D 330 . 12.971 −17.745 45.265 1.00 46.19 . 1 2280 ATOM O O PHE D 330 . 12.577 −18.738 44.649 1.00 46.98 . 1 2281 ATOM C CB PHE D 330 . 13.917 −15.580 44.474 1.00 45.42 . 1 2282 ATOM C CG PHE D 330 . 15.027 −16.462 43.979 1.00 47.03 . 1 2283 ATOM C CD1 PHE D 330 . 14.928 −17.102 42.747 1.00 47.09 . 1 2284 ATOM C CD2 PHE D 330 . 16.155 −16.683 44.766 1.00 46.71 . 1 2285 ATOM C CE1 PHE D 330 . 15.940 −17.955 42.304 1.00 49.29 . 1 2286 ATOM C CE2 PHE D 330 . 17.171 −17.533 44.336 1.00 48.20 . 1 2287 ATOM C CZ PHE D 330 . 17.064 −18.172 43.102 1.00 49.37 . 1 2288 ATOM N N ILE D 331 . 13.707 −17.823 46.367 1.00 46.36 . 1 2289 ATOM C CA ILE D 331 . 14.137 −19.110 46.896 1.00 48.07 . 1 2290 ATOM C C ILE D 331 . 13.006 −19.968 47.446 1.00 48.06 . 1 2291 ATOM O O ILE D 331 . 13.115 −21.195 47.486 1.00 48.43 . 1 2292 ATOM C CB ILE D 331 . 15.201 −18.926 48.011 1.00 49.10 . 1 2293 ATOM C CG1 ILE D 331 . 15.698 −20.294 48.493 1.00 49.80 . 1 2294 ATOM C CG2 ILE D 331 . 14.609 −18.140 49.168 1.00 48.64 . 1 2295 ATOM C CD1 ILE D 331 . 16.757 −20.226 49.573 1.00 50.88 . 1 2296 ATOM N N THR D 332 . 11.913 −19.337 47.854 1.00 47.37 . 1 2297 ATOM C CA THR D 332 . 10.813 −20.092 48.426 1.00 48.26 . 1 2298 ATOM C C THR D 332 . 9.856 −20.729 47.424 1.00 48.21 . 1 2299 ATOM O O THR D 332 . 9.607 −21.933 47.487 1.00 48.50 . 1 2300 ATOM C CB THR D 332 . 9.996 −19.224 49.404 1.00 48.61 . 1 2301 ATOM O OG1 THR D 332 . 9.074 −20.056 50.110 1.00 52.99 . 1 2302 ATOM C CG2 THR D 332 . 9.219 −18.152 48.662 1.00 48.19 . 1 2303 ATOM N N VAL D 333 . 9.324 −19.930 46.505 1.00 47.74 . 1 2304 ATOM C CA VAL D 333 . 8.371 −20.429 45.524 1.00 47.78 . 1 2305 ATOM C C VAL D 333 . 8.720 −20.011 44.102 1.00 47.63 . 1 2306 ATOM O O VAL D 333 . 7.962 −20.277 43.161 1.00 47.35 . 1 2307 ATOM C CB VAL D 333 . 6.954 −19.910 45.833 1.00 48.53 . 1 2308 ATOM C CG1 VAL D 333 . 6.596 −20.207 47.279 1.00 49.11 . 1 2309 ATOM C CG2 VAL D 333 . 6.876 −18.415 45.560 1.00 47.25 . 1 2310 ATOM N N GLY D 334 . 9.864 −19.356 43.944 1.00 46.71 . 1 2311 ATOM C CA GLY D 334 . 10.259 −18.899 42.625 1.00 44.91 . 1 2312 ATOM C C GLY D 334 . 9.421 −17.699 42.225 1.00 43.71 . 1 2313 ATOM O O GLY D 334 . 9.198 −17.444 41.040 1.00 43.94 . 1 2314 ATOM N N GLY D 335 . 8.934 −16.973 43.228 1.00 41.26 . 1 2315 ATOM C CA GLY D 335 . 8.139 −15.787 42.972 1.00 37.56 . 1 2316 ATOM C C GLY D 335 . 9.063 −14.589 42.864 1.00 35.94 . 1 2317 ATOM O O GLY D 335 . 10.277 −14.756 42.756 1.00 34.99 . 1 2318 ATOM N N ARG D 336 . 8.510 −13.382 42.902 1.00 34.39 . 1 2319 ATOM C CA ARG D 336 . 9.341 −12.194 42.795 1.00 33.98 . 1 2320 ATOM C C ARG D 336 . 8.572 −10.931 43.161 1.00 31.19 . 1 2321 ATOM O O ARG D 336 . 7.348 −10.875 43.042 1.00 30.90 . 1 2322 ATOM C CB ARG D 336 . 9.881 −12.061 41.362 1.00 37.40 . 1 2323 ATOM C CG ARG D 336 . 8.851 −11.509 40.375 1.00 43.50 . 1 2324 ATOM C CD ARG D 336 . 9.322 −11.536 38.925 1.00 49.69 . 1 2325 ATOM N NE ARG D 336 . 8.840 −12.716 38.208 1.00 55.68 . 1 2326 ATOM C CZ ARG D 336 . 9.384 −13.926 38.295 1.00 58.13 . 1 2327 ATOM N NH1 ARG D 336 . 10.444 −14.129 39.068 1.00 59.14 . 1 2328 ATOM N NH2 ARG D 336 . 8.860 −14.939 37.615 1.00 58.84 . 1 2329 ATOM N N GLU D 337 . 9.290 −9.915 43.621 1.00 29.51 . 1 2330 ATOM C CA GLU D 337 . 8.644 −8.657 43.949 1.00 26.91 . 1 2331 ATOM C C GLU D 337 . 8.869 −7.776 42.727 1.00 28.68 . 1 2332 ATOM O O GLU D 337 . 9.799 −8.006 41.954 1.00 28.90 . 1 2333 ATOM C CB GLU D 337 . 9.248 −8.024 45.203 1.00 28.50 . 1 2334 ATOM C CG GLU D 337 . 8.948 −8.787 46.513 1.00 24.88 . 1 2335 ATOM C CD GLU D 337 . 7.481 −9.122 46.692 1.00 27.16 . 1 2336 ATOM O OE1 GLU D 337 . 6.614 −8.279 46.360 1.00 29.87 . 1 2337 ATOM O OE2 GLU D 337 . 7.174 −10.230 47.184 1.00 29.53 . 1 2338 ATOM N N ARG D 338 . 8.026 −6.770 42.550 1.00 29.08 . 1 2339 ATOM C CA ARG D 338 . 8.145 −5.911 41.377 1.00 30.35 . 1 2340 ATOM C C ARG D 338 . 8.105 −4.419 41.684 1.00 29.54 . 1 2341 ATOM O O ARG D 338 . 7.580 −3.988 42.716 1.00 27.47 . 1 2342 ATOM C CB ARG D 338 . 7.025 −6.244 40.382 1.00 32.08 . 1 2343 ATOM C CG ARG D 338 . 7.061 −7.662 39.793 1.00 33.82 . 1 2344 ATOM C CD ARG D 338 . 5.861 −7.878 38.852 1.00 34.47 . 1 2345 ATOM N NE ARG D 338 . 5.986 −9.048 37.977 1.00 34.02 . 1 2346 ATOM C CZ ARG D 338 . 5.549 −10.272 38.270 1.00 36.09 . 1 2347 ATOM N NH1 ARG D 338 . 4.949 −10.515 39.432 1.00 32.49 . 1 2348 ATOM N NH2 ARG D 338 . 5.698 −11.256 37.389 1.00 36.13 . 1 2349 ATOM N N THR D 339 . 8.651 −3.641 40.755 1.00 29.46 . 1 2350 ATOM C CA THR D 339 . 8.683 −2.193 40.862 1.00 31.78 . 1 2351 ATOM C C THR D 339 . 7.332 −1.640 40.411 1.00 32.95 . 1 2352 ATOM O O THR D 339 . 6.514 −2.359 39.825 1.00 31.90 . 1 2353 ATOM C CB THR D 339 . 9.759 −1.593 39.938 1.00 32.09 . 1 2354 ATOM O OG1 THR D 339 . 9.413 −1.882 38.581 1.00 34.28 . 1 2355 ATOM C CG2 THR D 339 . 11.128 −2.188 40.233 1.00 33.26 . 1 2356 ATOM N N GLU D 340 . 7.106 −0.360 40.680 1.00 33.54 . 1 2357 ATOM C CA GLU D 340 . 5.860 0.289 40.294 1.00 37.11 . 1 2358 ATOM C C GLU D 340 . 5.669 0.209 38.782 1.00 37.69 . 1 2359 ATOM O O GLU D 340 . 4.586 −0.132 38.300 1.00 38.68 . 1 2360 ATOM C CB GLU D 340 . 5.873 1.757 40.725 1.00 38.71 . 1 2361 ATOM C CG GLU D 340 . 4.553 2.470 40.499 1.00 41.56 . 1 2362 ATOM C CD GLU D 340 . 4.613 3.938 40.863 1.00 43.76 . 1 2363 ATOM O OE1 GLU D 340 . 5.110 4.259 41.963 1.00 44.12 . 1 2364 ATOM O OE2 GLU D 340 . 4.154 4.770 40.052 1.00 44.77 . 1 2365 ATOM N N LYS D 341 . 6.726 0.514 38.034 1.00 39.82 . 1 2366 ATOM C CA LYS D 341 . 6.655 0.475 36.573 1.00 40.15 . 1 2367 ATOM C C LYS D 341 . 6.365 −0.924 36.059 1.00 39.13 . 1 2368 ATOM O O LYS D 341 . 5.700 −1.087 35.038 1.00 37.44 . 1 2369 ATOM C CB LYS D 341 . 7.958 0.984 35.954 1.00 41.73 . 1 2370 ATOM C CG LYS D 341 . 8.248 2.445 36.254 1.00 46.25 . 1 2371 ATOM C CD LYS D 341 . 9.508 2.925 35.546 1.00 49.47 . 1 2372 ATOM C CE LYS D 341 . 9.804 4.383 35.891 1.00 51.59 . 1 2373 ATOM N NZ LYS D 341 . 10.998 4.910 35.166 1.00 54.57 . 1 2374 ATOM N N GLN D 342 . 6.865 −1.936 36.760 1.00 38.14 . 1 2375 ATOM C CA GLN D 342 . 6.636 −3.314 36.340 1.00 37.00 . 1 2376 ATOM C C GLN D 342 . 5.170 −3.704 36.490 1.00 36.20 . 1 2377 ATOM O O GLN D 342 . 4.635 −4.435 35.658 1.00 36.50 . 1 2378 ATOM C CB GLN D 342 . 7.541 −4.274 37.120 1.00 37.85 . 1 2379 ATOM C CG GLN D 342 . 9.017 −4.135 36.755 1.00 40.47 . 1 2380 ATOM C CD GLN D 342 . 9.917 −5.082 37.530 1.00 42.52 . 1 2381 ATOM O OE1 GLN D 342 . 9.786 −5.228 38.743 1.00 39.75 . 1 2382 ATOM N NE2 GLN D 342 . 10.848 −5.719 36.829 1.00 45.16 . 1 2383 ATOM N N TYR D 343 . 4.518 −3.220 37.545 1.00 35.89 . 1 2384 ATOM C CA TYR D 343 . 3.102 −3.518 37.745 1.00 34.81 . 1 2385 ATOM C C TYR D 343 . 2.279 −2.762 36.703 1.00 36.14 . 1 2386 ATOM O O TYR D 343 . 1.308 −3.290 36.159 1.00 33.76 . 1 2387 ATOM C CB TYR D 343 . 2.652 −3.125 39.159 1.00 34.77 . 1 2388 ATOM C CG TYR D 343 . 2.966 −4.181 40.198 1.00 32.03 . 1 2389 ATOM C CD1 TYR D 343 . 3.887 −3.939 41.218 1.00 32.30 . 1 2390 ATOM C CD2 TYR D 343 . 2.359 −5.440 40.139 1.00 32.32 . 1 2391 ATOM C CE1 TYR D 343 . 4.199 −4.932 42.155 1.00 30.17 . 1 2392 ATOM C CE2 TYR D 343 . 2.663 −6.436 41.070 1.00 30.98 . 1 2393 ATOM C CZ TYR D 343 . 3.584 −6.176 42.072 1.00 30.84 . 1 2394 ATOM O OH TYR D 343 . 3.887 −7.171 42.982 1.00 29.45 . 1 2395 ATOM N N GLU D 344 . 2.670 −1.523 36.426 1.00 37.74 . 1 2396 ATOM C CA GLU D 344 . 1.958 −0.734 35.427 1.00 41.42 . 1 2397 ATOM C C GLU D 344 . 2.067 −1.427 34.068 1.00 40.58 . 1 2398 ATOM O O GLU D 344 . 1.121 −1.436 33.283 1.00 41.35 . 1 2399 ATOM C CB GLU D 344 . 2.537 0.678 35.355 1.00 43.09 . 1 2400 ATOM C CG GLU D 344 . 1.947 1.539 34.246 1.00 47.33 . 1 2401 ATOM C CD GLU D 344 . 2.325 2.996 34.391 1.00 50.15 . 1 2402 ATOM O OE1 GLU D 344 . 3.482 3.268 34.764 1.00 51.16 . 1 2403 ATOM O OE2 GLU D 344 . 1.470 3.871 34.126 1.00 53.96 . 1 2404 ATOM N N LYS D 345 . 3.225 −2.020 33.806 1.00 41.90 . 1 2405 ATOM C CA LYS D 345 . 3.457 −2.730 32.556 1.00 43.31 . 1 2406 ATOM C C LYS D 345 . 2.470 −3.888 32.467 1.00 43.24 . 1 2407 ATOM O O LYS D 345 . 1.780 −4.060 31.458 1.00 42.67 . 1 2408 ATOM C CB LYS D 345 . 4.897 −3.249 32.516 1.00 45.47 . 1 2409 ATOM C CG LYS D 345 . 5.369 −3.717 31.154 1.00 48.72 . 1 2410 ATOM C CD LYS D 345 . 6.888 −3.829 31.125 1.00 51.09 . 1 2411 ATOM C CE LYS D 345 . 7.408 −4.118 29.725 1.00 52.43 . 1 2412 ATOM N NZ LYS D 345 . 6.991 −5.461 29.233 1.00 54.51 . 1 2413 ATOM N N LEU D 346 . 2.399 −4.681 33.531 1.00 41.34 . 1 2414 ATOM C CA LEU D 346 . 1.481 −5.811 33.573 1.00 40.53 . 1 2415 ATOM C C LEU D 346 . 0.058 −5.306 33.370 1.00 40.43 . 1 2416 ATOM O O LEU D 346 . −0.759 −5.959 32.725 1.00 39.29 . 1 2417 ATOM C CB LEU D 346 . 1.588 −6.528 34.923 1.00 40.86 . 1 2418 ATOM C CG LEU D 346 . 2.407 −7.820 35.011 1.00 41.28 . 1 2419 ATOM C CD1 LEU D 346 . 3.702 −7.699 34.242 1.00 42.87 . 1 2420 ATOM C CD2 LEU D 346 . 2.678 −8.128 36.479 1.00 39.69 . 1 2421 ATOM N N SER D 347 . −0.222 −4.134 33.927 1.00 40.19 . 1 2422 ATOM C CA SER D 347 . −1.536 −3.514 33.835 1.00 42.16 . 1 2423 ATOM C C SER D 347 . −1.939 −3.242 32.389 1.00 43.49 . 1 2424 ATOM O O SER D 347 . −3.033 −3.608 31.958 1.00 43.09 . 1 2425 ATOM C CB SER D 347 . −1.538 −2.202 34.617 1.00 44.09 . 1 2426 ATOM O OG SER D 347 . −2.724 −1.464 34.388 1.00 48.19 . 1 2427 ATOM N N LYS D 348 . −1.050 −2.596 31.644 1.00 44.39 . 1 2428 ATOM C CA LYS D 348 . −1.321 −2.265 30.247 1.00 44.89 . 1 2429 ATOM C C LYS D 348 . −1.374 −3.495 29.350 1.00 44.92 . 1 2430 ATOM O O LYS D 348 . −2.257 −3.611 28.501 1.00 44.18 . 1 2431 ATOM C CB LYS D 348 . −0.270 −1.280 29.734 1.00 45.74 . 1 2432 ATOM C CG LYS D 348 . −0.406 0.098 30.356 1.00 49.72 . 1 2433 ATOM C CD LYS D 348 . 0.673 1.067 29.888 1.00 52.02 . 1 2434 ATOM C CE LYS D 348 . 2.010 0.784 30.549 1.00 53.10 . 1 2435 ATOM N NZ LYS D 348 . 3.030 1.789 30.143 1.00 54.34 . 1 2436 ATOM N N LEU D 349 . −0.435 −4.415 29.543 1.00 44.00 . 1 2437 ATOM C CA LEU D 349 . −0.396 −5.630 28.738 1.00 43.93 . 1 2438 ATOM C C LEU D 349 . −1.608 −6.512 28.999 1.00 44.50 . 1 2439 ATOM O O LEU D 349 . −1.896 −7.426 28.222 1.00 44.66 . 1 2440 ATOM C CB LEU D 349 . 0.884 −6.423 29.023 1.00 43.50 . 1 2441 ATOM C CG LEU D 349 . 2.200 −5.794 28.560 1.00 44.80 . 1 2442 ATOM C CD1 LEU D 349 . 3.367 −6.665 28.989 1.00 43.58 . 1 2443 ATOM C CD2 LEU D 349 . 2.184 −5.632 27.043 1.00 44.88 . 1 2444 ATOM N N SER D 350 . −2.318 −6.231 30.091 1.00 43.69 . 1 2445 ATOM C CA SER D 350 . −3.501 −7.004 30.467 1.00 43.74 . 1 2446 ATOM C C SER D 350 . −4.808 −6.411 29.947 1.00 43.00 . 1 2447 ATOM O O SER D 350 . −5.866 −7.021 30.091 1.00 43.03 . 1 2448 ATOM C CB SER D 350 . −3.579 −7.153 31.991 1.00 42.43 . 1 2449 ATOM O OG SER D 350 . −2.565 −8.024 32.457 1.00 43.02 . 1 2450 ATOM N N GLY D 351 . −4.735 −5.219 29.365 1.00 43.18 . 1 2451 ATOM C CA GLY D 351 . −5.927 −4.597 28.816 1.00 43.54 . 1 2452 ATOM C C GLY D 351 . −6.528 −3.460 29.610 1.00 43.88 . 1 2453 ATOM O O GLY D 351 . −7.505 −2.851 29.176 1.00 44.30 . 1 2454 ATOM N N PHE D 352 . −5.963 −3.163 30.774 1.00 43.55 . 1 2455 ATOM C CA PHE D 352 . −6.488 −2.082 31.594 1.00 42.62 . 1 2456 ATOM C C PHE D 352 . −6.082 −0.731 31.020 1.00 43.47 . 1 2457 ATOM O O PHE D 352 . −4.999 −0.588 30.459 1.00 44.41 . 1 2458 ATOM C CB PHE D 352 . −6.013 −2.245 33.041 1.00 40.19 . 1 2459 ATOM C CG PHE D 352 . −6.525 −3.497 33.690 1.00 37.80 . 1 2460 ATOM C CD1 PHE D 352 . −5.889 −4.718 33.474 1.00 37.07 . 1 2461 ATOM C CD2 PHE D 352 . −7.687 −3.469 34.453 1.00 37.04 . 1 2462 ATOM C CE1 PHE D 352 . −6.407 −5.898 34.006 1.00 39.03 . 1 2463 ATOM C CE2 PHE D 352 . −8.217 −4.636 34.987 1.00 38.73 . 1 2464 ATOM C CZ PHE D 352 . −7.576 −5.859 34.763 1.00 39.08 . 1 2465 ATOM N N SER D 353 . −6.962 0.255 31.169 1.00 44.77 . 1 2466 ATOM C CA SER D 353 . −6.741 1.590 30.625 1.00 46.01 . 1 2467 ATOM C C SER D 353 . −5.959 2.553 31.503 1.00 46.65 . 1 2468 ATOM O O SER D 353 . −5.223 3.398 30.992 1.00 46.49 . 1 2469 ATOM C CB SER D 353 . −8.085 2.242 30.290 1.00 45.97 . 1 2470 ATOM O OG SER D 353 . −8.768 2.623 31.476 1.00 45.62 . 1 2471 ATOM N N LYS D 354 . −6.127 2.443 32.817 1.00 45.64 . 1 2472 ATOM C CA LYS D 354 . −5.442 3.348 33.728 1.00 45.98 . 1 2473 ATOM C C LYS D 354 . −4.775 2.636 34.900 1.00 46.18 . 1 2474 ATOM O O LYS D 354 . −5.333 1.703 35.478 1.00 46.06 . 1 2475 ATOM C CB LYS D 354 . −6.429 4.381 34.273 1.00 46.79 . 1 2476 ATOM C CG LYS D 354 . −5.789 5.437 35.166 1.00 49.65 . 1 2477 ATOM C CD LYS D 354 . −6.821 6.316 35.867 1.00 51.86 . 1 2478 ATOM C CE LYS D 354 . −7.680 7.106 34.887 1.00 54.94 . 1 2479 ATOM N NZ LYS D 354 . −8.649 6.253 34.138 1.00 56.97 . 1 2480 ATOM N N PHE D 355 . −3.578 3.099 35.243 1.00 45.33 . 1 2481 ATOM C CA PHE D 355 . −2.821 2.542 36.353 1.00 44.31 . 1 2482 ATOM C C PHE D 355 . −2.495 3.655 37.329 1.00 44.26 . 1 2483 ATOM O O PHE D 355 . −2.229 4.789 36.928 1.00 45.42 . 1 2484 ATOM C CB PHE D 355 . −1.509 1.922 35.868 1.00 43.27 . 1 2485 ATOM C CG PHE D 355 . −0.555 1.587 36.985 1.00 42.91 . 1 2486 ATOM C CD1 PHE D 355 . −0.727 0.436 37.743 1.00 42.65 . 1 2487 ATOM C CD2 PHE D 355 . 0.493 2.445 37.301 1.00 43.00 . 1 2488 ATOM C CE1 PHE D 355 . 0.135 0.142 38.802 1.00 41.62 . 1 2489 ATOM C CE2 PHE D 355 . 1.358 2.160 38.358 1.00 43.81 . 1 2490 ATOM C CZ PHE D 355 . 1.178 1.007 39.107 1.00 41.84 . 1 2491 ATOM N N GLN D 356 . −2.512 3.326 38.614 1.00 44.34 . 1 2492 ATOM C CA GLN D 356 . −2.189 4.299 39.642 1.00 43.78 . 1 2493 ATOM C C GLN D 356 . −1.993 3.638 40.997 1.00 42.63 . 1 2494 ATOM O O GLN D 356 . −2.600 2.610 41.299 1.00 42.94 . 1 2495 ATOM C CB GLN D 356 . −3.290 5.355 39.759 1.00 45.34 . 1 2496 ATOM C CG GLN D 356 . −4.618 4.827 40.275 1.00 49.09 . 1 2497 ATOM C CD GLN D 356 . −5.642 5.930 40.471 1.00 52.29 . 1 2498 ATOM O OE1 GLN D 356 . −6.755 5.684 40.935 1.00 53.80 . 1 2499 ATOM N NE2 GLN D 356 . −5.268 7.155 40.115 1.00 52.60 . 1 2500 ATOM N N VAL D 357 . −1.118 4.228 41.801 1.00 40.69 . 1 2501 ATOM C CA VAL D 357 . −0.870 3.741 43.145 1.00 38.09 . 1 2502 ATOM C C VAL D 357 . −1.781 4.616 43.986 1.00 37.13 . 1 2503 ATOM O O VAL D 357 . −1.545 5.820 44.100 1.00 38.94 . 1 2504 ATOM C CB VAL D 357 . 0.593 3.980 43.576 1.00 38.26 . 1 2505 ATOM C CG1 VAL D 357 . 0.794 3.528 45.026 1.00 37.03 . 1 2506 ATOM C CG2 VAL D 357 . 1.536 3.237 42.643 1.00 38.39 . 1 2507 ATOM N N ALA D 358 . −2.834 4.033 44.551 1.00 35.20 . 1 2508 ATOM C CA ALA D 358 . −3.765 4.802 45.369 1.00 34.17 . 1 2509 ATOM C C ALA D 358 . −3.125 5.264 46.672 1.00 35.39 . 1 2510 ATOM O O ALA D 358 . −3.366 6.379 47.133 1.00 34.95 . 1 2511 ATOM C CB ALA D 358 . −5.011 3.977 45.670 1.00 32.72 . 1 2512 ATOM N N CYS D 359 . −2.314 4.396 47.269 1.00 34.96 . 1 2513 ATOM C CA CYS D 359 . −1.650 4.715 48.527 1.00 34.02 . 1 2514 ATOM C C CYS D 359 . −0.624 3.641 48.872 1.00 32.93 . 1 2515 ATOM O O CYS D 359 . −0.483 2.657 48.152 1.00 31.19 . 1 2516 ATOM C CB CYS D 359 . −2.682 4.825 49.651 1.00 34.33 . 1 2517 ATOM S SG CYS D 359 . −3.704 3.340 49.889 1.00 37.87 . 1 2518 ATOM N N ARG D 360 . 0.094 3.854 49.971 1.00 33.33 . 1 2519 ATOM C CA ARG D 360 . 1.115 2.922 50.437 1.00 33.85 . 1 2520 ATOM C C ARG D 360 . 1.053 2.819 51.954 1.00 32.71 . 1 2521 ATOM O O ARG D 360 . 0.883 3.825 52.653 1.00 31.06 . 1 2522 ATOM C CB ARG D 360 . 2.524 3.409 50.063 1.00 36.57 . 1 2523 ATOM C CG ARG D 360 . 2.923 3.310 48.598 1.00 41.23 . 1 2524 ATOM C CD ARG D 360 . 4.084 4.271 48.328 1.00 44.69 . 1 2525 ATOM N NE ARG D 360 . 4.734 4.075 47.033 1.00 47.80 . 1 2526 ATOM C CZ ARG D 360 . 5.618 3.115 46.788 1.00 48.61 . 1 2527 ATOM N NH1 ARG D 360 . 5.953 2.265 47.750 1.00 51.29 . 1 2528 ATOM N NH2 ARG D 360 . 6.177 3.008 45.593 1.00 49.46 . 1 2529 ATOM N N ALA D 361 . 1.193 1.600 52.459 1.00 30.86 . 1 2530 ATOM C CA ALA D 361 . 1.207 1.376 53.892 1.00 29.64 . 1 2531 ATOM C C ALA D 361 . 2.655 1.022 54.213 1.00 28.21 . 1 2532 ATOM O O ALA D 361 . 3.346 0.423 53.393 1.00 28.00 . 1 2533 ATOM C CB ALA D 361 . 0.280 0.224 54.267 1.00 29.81 . 1 2534 ATOM N N PHE D 362 . 3.124 1.422 55.388 1.00 27.92 . 1 2535 ATOM C CA PHE D 362 . 4.491 1.125 55.796 1.00 28.80 . 1 2536 ATOM C C PHE D 362 . 5.503 1.635 54.762 1.00 29.57 . 1 2537 ATOM O O PHE D 362 . 6.583 1.061 54.595 1.00 27.44 . 1 2538 ATOM C CB PHE D 362 . 4.648 −0.390 55.989 1.00 28.87 . 1 2539 ATOM C CG PHE D 362 . 3.441 −1.051 56.606 1.00 30.08 . 1 2540 ATOM C CD1 PHE D 362 . 2.915 −2.218 56.054 1.00 31.09 . 1 2541 ATOM C CD2 PHE D 362 . 2.815 −0.501 57.720 1.00 31.41 . 1 2542 ATOM C CE1 PHE D 362 . 1.782 −2.825 56.601 1.00 30.21 . 1 2543 ATOM C CE2 PHE D 362 . 1.684 −1.100 58.275 1.00 30.68 . 1 2544 ATOM C CZ PHE D 362 . 1.166 −2.265 57.711 1.00 32.43 . 1 2545 ATOM N N ASN D 363 . 5.139 2.712 54.067 1.00 28.84 . 1 2546 ATOM C CA ASN D 363 . 5.994 3.319 53.053 1.00 31.97 . 1 2547 ATOM C C ASN D 363 . 6.501 2.281 52.064 1.00 32.14 . 1 2548 ATOM O O ASN D 363 . 7.569 2.453 51.473 1.00 33.62 . 1 2549 ATOM C CB ASN D 363 . 7.201 3.993 53.713 1.00 33.71 . 1 2550 ATOM C CG ASN D 363 . 6.806 5.019 54.754 1.00 37.26 . 1 2551 ATOM O OD1 ASN D 363 . 7.598 5.357 55.633 1.00 38.85 . 1 2552 ATOM N ND2 ASN D 363 . 5.582 5.528 54.658 1.00 36.22 . 1 2553 ATOM N N SER D 364 . 5.746 1.204 51.871 1.00 31.92 . 1 2554 ATOM C CA SER D 364 . 6.207 0.159 50.965 1.00 30.33 . 1 2555 ATOM C C SER D 364 . 5.136 −0.789 50.446 1.00 29.25 . 1 2556 ATOM O O SER D 364 . 5.294 −1.354 49.364 1.00 33.16 . 1 2557 ATOM C CB SER D 364 . 7.301 −0.656 51.652 1.00 29.88 . 1 2558 ATOM O OG SER D 364 . 6.826 −1.149 52.893 1.00 30.90 . 1 2559 ATOM N N LEU D 365 . 4.072 −0.996 51.217 1.00 29.33 . 1 2560 ATOM C CA LEU D 365 . 3.000 −1.883 50.778 1.00 27.90 . 1 2561 ATOM C C LEU D 365 . 2.021 −1.061 49.959 1.00 26.38 . 1 2562 ATOM O O LEU D 365 . 1.248 −0.274 50.503 1.00 26.52 . 1 2563 ATOM C CB LEU D 365 . 2.270 −2.505 51.970 1.00 27.07 . 1 2564 ATOM C CG LEU D 365 . 1.131 −3.455 51.570 1.00 26.37 . 1 2565 ATOM C CD1 LEU D 365 . 1.688 −4.627 50.764 1.00 25.73 . 1 2566 ATOM C CD2 LEU D 365 . 0.415 −3.951 52.813 1.00 26.70 . 1 2567 ATOM N N GLY D 366 . 2.045 −1.253 48.648 1.00 29.66 . 1 2568 ATOM C CA GLY D 366 . 1.170 −0.470 47.802 1.00 29.81 . 1 2569 ATOM C C GLY D 366 . −0.202 −1.043 47.533 1.00 31.07 . 1 2570 ATOM O O GLY D 366 . −0.422 −2.251 47.596 1.00 30.53 . 1 2571 ATOM N N VAL D 367 . −1.137 −0.141 47.264 1.00 30.70 . 1 2572 ATOM C CA VAL D 367 . −2.498 −0.504 46.914 1.00 30.84 . 1 2573 ATOM C C VAL D 367 . −2.647 0.146 45.550 1.00 32.28 . 1 2574 ATOM O O VAL D 367 . −2.900 1.349 45.450 1.00 33.93 . 1 2575 ATOM C CB VAL D 367 . −3.535 0.092 47.888 1.00 32.37 . 1 2576 ATOM C CG1 VAL D 367 . −4.947 −0.241 47.415 1.00 31.13 . 1 2577 ATOM C CG2 VAL D 367 . −3.317 −0.467 49.288 1.00 29.43 . 1 2578 ATOM N N MET D 368 . −2.437 −0.650 44.507 1.00 31.82 . 1 2579 ATOM C CA MET D 368 . −2.515 −0.172 43.136 1.00 31.05 . 1 2580 ATOM C C MET D 368 . −3.865 −0.506 42.520 1.00 32.64 . 1 2581 ATOM O O MET D 368 . −4.497 −1.491 42.888 1.00 30.42 . 1 2582 ATOM C CB MET D 368 . −1.384 −0.798 42.318 1.00 31.33 . 1 2583 ATOM C CG MET D 368 . 0.011 −0.349 42.765 1.00 28.53 . 1 2584 ATOM S SD MET D 368 . 1.318 −1.455 42.225 1.00 32.02 . 1 2585 ATOM C CE MET D 368 . 1.251 −2.697 43.572 1.00 30.67 . 1 2586 ATOM N N GLU D 369 . −4.312 0.330 41.588 1.00 34.05 . 1 2587 ATOM C CA GLU D 369 . −5.590 0.102 40.926 1.00 34.20 . 1 2588 ATOM C C GLU D 369 . −5.404 0.041 39.412 1.00 35.87 . 1 2589 ATOM O O GLU D 369 . −4.728 0.887 38.822 1.00 35.86 . 1 2590 ATOM C CB GLU D 369 . −6.585 1.217 41.273 1.00 34.90 . 1 2591 ATOM C CG GLU D 369 . −6.812 1.435 42.764 1.00 35.98 . 1 2592 ATOM C CD GLU D 369 . −7.729 2.617 43.046 1.00 37.66 . 1 2593 ATOM O OE1 GLU D 369 . −7.550 3.678 42.405 1.00 38.69 . 1 2594 ATOM O OE2 GLU D 369 . −8.619 2.496 43.912 1.00 38.42 . 1 2595 ATOM N N PHE D 370 . −5.988 −0.983 38.799 1.00 35.90 . 1 2596 ATOM C CA PHE D 370 . −5.935 −1.164 37.355 1.00 36.81 . 1 2597 ATOM C C PHE D 370 . −7.359 −0.888 36.871 1.00 38.13 . 1 2598 ATOM O O PHE D 370 . −8.263 −1.683 37.126 1.00 38.25 . 1 2599 ATOM C CB PHE D 370 . −5.582 −2.610 36.978 1.00 35.77 . 1 2600 ATOM C CG PHE D 370 . −4.196 −3.052 37.378 1.00 34.65 . 1 2601 ATOM C CD1 PHE D 370 . −3.746 −4.324 37.018 1.00 34.23 . 1 2602 ATOM C CD2 PHE D 370 . −3.340 −2.219 38.090 1.00 34.27 . 1 2603 ATOM C CE1 PHE D 370 . −2.471 −4.761 37.356 1.00 33.03 . 1 2604 ATOM C CE2 PHE D 370 . −2.057 −2.647 38.434 1.00 31.68 . 1 2605 ATOM C CZ PHE D 370 . −1.624 −3.921 38.065 1.00 31.97 . 1 2606 ATOM N N TYR D 371 . −7.574 0.231 36.193 1.00 39.85 . 1 2607 ATOM C CA TYR D 371 . −8.917 0.529 35.707 1.00 42.26 . 1 2608 ATOM C C TYR D 371 . −9.140 −0.065 34.323 1.00 43.59 . 1 2609 ATOM O O TYR D 371 . −8.279 0.029 33.449 1.00 44.41 . 1 2610 ATOM C CB TYR D 371 . −9.167 2.040 35.683 1.00 41.09 . 1 2611 ATOM C CG TYR D 371 . −9.309 2.647 37.060 1.00 40.66 . 1 2612 ATOM C CD1 TYR D 371 . −8.189 3.011 37.806 1.00 40.85 . 1 2613 ATOM C CD2 TYR D 371 . −10.567 2.820 37.635 1.00 40.90 . 1 2614 ATOM C CE1 TYR D 371 . −8.319 3.536 39.096 1.00 39.68 . 1 2615 ATOM C CE2 TYR D 371 . −10.709 3.337 38.919 1.00 40.20 . 1 2616 ATOM C CZ TYR D 371 . −9.584 3.692 39.644 1.00 40.45 . 1 2617 ATOM O OH TYR D 371 . −9.733 4.192 40.917 1.00 41.42 . 1 2618 ATOM N N LYS D 372 . −10.300 −0.688 34.140 1.00 45.07 . 1 2619 ATOM C CA LYS D 372 . −10.655 −1.309 32.871 1.00 47.61 . 1 2620 ATOM C C LYS D 372 . −10.647 −0.277 31.744 1.00 48.89 . 1 2621 ATOM O O LYS D 372 . −10.964 0.894 31.963 1.00 48.95 . 1 2622 ATOM C CB LYS D 372 . −12.042 −1.947 32.978 1.00 47.75 . 1 2623 ATOM C CG LYS D 372 . −12.376 −2.880 31.832 1.00 46.67 . 1 2624 ATOM C CD LYS D 372 . −13.717 −3.557 32.040 1.00 46.58 . 1 2625 ATOM C CE LYS D 372 . −13.964 −4.595 30.962 1.00 45.28 . 1 2626 ATOM N NZ LYS D 372 . −15.196 −5.376 31.223 1.00 48.37 . 1 2627 ATOM O OXT LYS D 372 . −10.343 −0.691 30.606 1.00 52.29 . 1 2628 #372 . TER # . . LYS D 372 . . . . . . . 1 2629 HETA N N SAH D 1699 . −5.182 −13.138 49.176 1.00 32.12 . 2 2630 HETA C CA SAH D 1699 . −4.392 −14.027 50.111 1.00 36.18 . 2 2631 HETA C CB SAH D 1699 . −3.353 −14.679 49.324 1.00 37.48 . 2 2632 HETA C CG SAH D 1699 . −2.296 −15.649 49.760 1.00 38.87 . 2 2633 HETA S SD SAH D 1699 . −1.508 −16.532 48.419 1.00 34.98 . 2 2634 HETA C C SAH D 1699 . −3.722 −13.124 51.209 1.00 35.76 . 2 2635 HETA O O SAH D 1699 . −3.424 −13.693 52.308 1.00 37.79 . 2 2636 HETA O OXT SAH D 1699 . −3.494 −11.922 50.923 1.00 33.64 . 2 2637 HETA C C5* SAH D 1699 . −2.906 −16.728 47.160 1.00 39.90 . 2 2638 HETA C C4* SAH D 1699 . −3.124 −17.510 46.944 1.00 36.25 . 2 2639 HETA O O4* SAH D 1699 . −3.395 −17.668 45.500 1.00 38.34 . 2 2640 HETA C C3* SAH D 1699 . −3.396 −18.872 47.633 1.00 36.45 . 2 2641 HETA O O3* SAH D 1699 . −4.607 −18.741 48.427 1.00 31.22 . 2 2642 HETA C C2* SAH D 1699 . −3.658 −19.756 46.445 1.00 35.33 . 2 2643 HETA O O2* SAH D 1699 . −4.766 −20.613 46.692 1.00 38.68 . 2 2644 HETA C C1* SAH D 1699 . −3.767 −19.010 45.160 1.00 36.83 . 2 2645 HETA N N9 SAH D 1699 . −4.049 −19.537 43.877 1.00 34.49 . 2 2646 HETA C C8 SAH D 1699 . −3.035 −20.198 43.220 1.00 35.63 . 2 2647 HETA N N7 SAH D 1699 . −3.403 −20.618 42.084 1.00 36.23 . 2 2648 HETA C C5 SAH D 1699 . −4.711 −20.231 41.959 1.00 34.10 . 2 2649 HETA C C6 SAH D 1699 . −5.687 −20.429 40.845 1.00 33.50 . 2 2650 HETA N N6 SAH D 1699 . −5.324 −21.072 39.751 1.00 33.24 . 2 2651 HETA N N1 SAH D 1699 . −6.940 −19.893 41.067 1.00 32.26 . 2 2652 HETA C C2 SAH D 1699 . −7.330 −19.209 42.222 1.00 35.18 . 2 2653 HETA N N3 SAH D 1699 . −6.448 −19.015 43.260 1.00 32.61 . 2 2654 HETA C C4 SAH D 1699 . −5.176 −19.544 43.065 1.00 33.61 . 2 2655 HETA C C1 HCC D 2000 A 6.643 −18.133 51.718 0.50 38.44 . 3 2656 HETA C C1 HCC D 2000 B 6.136 −19.825 51.293 0.50 47.12 . 3 2657 HETA C C2 HCC D 2000 A 7.392 −17.250 52.461 0.50 36.87 . 3 2658 HETA C C2 HCC D 2000 B 6.902 −18.957 52.048 0.50 47.13 . 3 2659 HETA C C3 HCC D 2000 A 6.938 −15.745 52.640 0.50 36.00 . 3 2660 HETA C C3 HCC D 2000 B 6.572 −17.406 52.100 0.50 46.59 . 3 2661 HETA C C4 HCC D 2000 A 5.760 −15.300 52.037 0.50 34.56 . 3 2662 HETA C C4 HCC D 2000 B 5.488 −16.917 51.369 0.50 46.36 . 3 2663 HETA C C5 HCC D 2000 A 4.908 −16.300 51.191 0.50 36.84 . 3 2664 HETA C C5 HCC D 2000 B 4.620 −17.895 50.513 0.50 47.21 . 3 2665 HETA C C6 HCC D 2000 A 5.344 −17.620 51.058 0.50 37.63 . 3 2666 HETA C C6 HCC D 2000 B 4.945 −19.250 50.495 0.50 48.02 . 3 2667 HETA C C7 HCC D 2000 A 5.247 −13.812 52.174 0.50 31.74 . 3 2668 HETA C C7 HCC D 2000 B 5.089 −15.401 51.367 0.50 44.21 . 3 2669 HETA C C8 HCC D 2000 A 5.993 −12.942 53.224 0.50 25.76 . 3 2670 HETA C C8 HCC D 2000 B 4.895 −14.763 52.765 0.50 40.94 . 3 2671 HETA C C9 HCC D 2000 A 5.462 −11.499 53.328 0.50 20.03 . 3 2672 HETA C C9 HCC D 2000 B 4.497 −13.275 52.709 0.50 37.79 . 3 2673 HETA O O10 HCC D 2000 A 3.763 −15.867 50.605 0.50 38.00 . 3 2674 HETA O O10 HCC D 2000 B 3.568 −17.405 49.806 0.50 48.73 . 3 2675 HETA C C11 HCC D 2000 A 5.838 −10.773 54.609 0.50 17.75 . 3 2676 HETA C C11 HCC D 2000 B 3.020 −13.033 52.936 0.50 34.78 . 3 2677 HETA C C12 HCC D 2000 A 5.738 −9.262 54.668 0.50 17.02 . 3 2678 HETA C C12 HCC D 2000 B 2.521 −12.666 54.316 0.50 33.92 . 3 2679 HETA C C13 HCC D 2000 A 6.124 −8.554 55.988 0.50 15.28 . 3 2680 HETA C C13 HCC D 2000 B 1.003 −12.430 54.511 0.50 32.06 . 3 2681 HETA C C14 HCC D 2000 A 6.549 −9.272 57.094 0.50 16.37 . 3 2682 HETA C C14 HCC D 2000 B 0.119 −12.550 53.457 0.50 32.29 . 3 2683 HETA C C15 HCC D 2000 A 6.647 −10.805 57.015 0.50 15.62 . 3 2684 HETA C C15 HCC D 2000 B 0.646 −12.925 52.056 0.50 31.89 . 3 2685 HETA C C16 HCC D 2000 A 6.323 −11.503 55.882 0.50 15.03 . 3 2686 HETA C C16 HCC D 2000 B 1.979 −13.148 51.807 0.50 34.29 . 3 2687 HETA O O17 HCC D 2000 A 4.321 −13.357 51.503 0.50 32.54 . 3 2688 HETA O O17 HCC D 2000 B 4.932 −14.757 50.335 0.50 45.19 . 3 2689 HETA O O18 HCC D 2000 A 6.876 −8.644 58.233 0.50 15.08 . 3 2690 HETA O O18 HCC D 2000 B −1.197 −12.343 53.644 0.50 32.04 . 3 2691 HETA O O19 HCC D 2000 A 7.069 −19.347 51.613 0.50 38.97 . 3 2692 HETA O O19 HCC D 2000 B 6.453 −21.073 51.293 0.50 46.56 . 3 2693 HETA O O HOH . 1 . −6.226 −11.966 46.798 1.00 29.44 . 4 2694 HETA O O HOH . 2 . 4.129 −8.141 47.890 1.00 25.12 . 4 2695 HETA O O HOH . 3 . −10.512 −12.972 51.201 1.00 30.54 . 4 2696 HETA O O HOH . 4 . 25.923 −11.033 57.970 1.00 29.37 . 4 2697 HETA O O HOH . 5 . 17.681 −18.706 68.273 1.00 32.60 . 4 2698 HETA O O HOH . 6 . −7.113 −11.918 50.272 1.00 26.21 . 4 2699 HETA O O HOH . 7 . 26.671 −12.883 59.805 1.00 25.33 . 4 2700 HETA O O HOH . 8 . 7.229 −12.195 70.734 1.00 26.83 . 4 2701 HETA O O HOH . 9 . 5.871 −6.764 44.528 1.00 26.99 . 4 2702 HETA O O HOH . 10 . −1.355 −9.656 43.677 1.00 30.63 . 4 2703 HETA O O HOH . 11 . 33.413 −10.148 60.060 1.00 28.79 . 4 2704 HETA O O HOH . 12 . 10.501 −17.586 67.358 1.00 31.33 . 4 2705 HETA O O HOH . 13 . 22.776 −5.196 61.157 1.00 28.85 . 4 2706 HETA O O HOH . 14 . 2.169 −9.449 52.070 1.00 34.70 . 4 2707 HETA O O HOH . 15 . 5.449 −9.329 41.861 1.00 29.95 . 4 2708 HETA O O HOH . 16 . −1.359 −2.478 61.300 1.00 28.54 . 4 2709 HETA O O HOH . 17 . 15.704 −2.732 46.168 1.00 30.40 . 4 2710 HETA O O HOH . 18 . 1.616 −14.956 48.649 1.00 29.14 . 4 2711 HETA O O HOH . 19 . 6.301 −17.876 67.386 1.00 33.07 . 4 2712 HETA O O HOH . 20 . 0.270 −0.300 61.452 1.00 36.27 . 4 2713 HETA O O HOH . 22 . 8.965 1.467 41.980 1.00 32.13 . 4 2714 HETA O O HOH . 23 . 0.433 −16.351 66.422 1.00 42.62 . 4 2715 HETA O O HOH . 24 . −19.458 −18.052 53.542 1.00 29.35 . 4 2716 HETA O O HOH . 25 . −1.490 −9.656 63.699 1.00 29.12 . 4 2717 HETA O O HOH . 26 . 9.136 1.692 39.196 1.00 36.46 . 4 2718 HETA O O HOH . 27 . 5.394 0.840 32.950 1.00 45.04 . 4 2719 HETA O O HOH . 28 . 39.162 6.533 60.291 1.00 42.24 . 4 2720 HETA O O HOH . 29 . 6.508 −11.154 50.016 1.00 33.35 . 4 2721 HETA O O HOH . 30 . −8.562 −13.840 52.962 1.00 36.60 . 4 2722 HETA O O HOH . 31 . 16.982 −8.178 55.472 1.00 33.18 . 4 2723 HETA O O HOH . 32 . −1.209 −17.139 43.634 1.00 31.06 . 4 2724 HETA O O HOH . 33 . 6.970 −12.497 73.478 1.00 29.89 . 4 2725 HETA O O HOH . 34 . 11.258 −22.002 64.358 1.00 34.15 . 4 2726 HETA O O HOH . 35 . 4.556 −18.855 63.141 1.00 33.31 . 4 2727 HETA O O HOH . 36 . −5.240 −14.940 53.847 1.00 41.00 . 4 2728 HETA O O HOH . 37 . 2.368 −4.434 72.329 1.00 31.97 . 4 2729 HETA O O HOH . 38 . 20.015 2.266 79.603 1.00 44.04 . 4 2730 HETA O O HOH . 39 . 11.295 −0.695 37.010 1.00 39.42 . 4 2731 HETA O O HOH . 40 . 12.854 4.225 48.224 1.00 37.98 . 4 2732 HETA O O HOH . 41 . 22.582 −2.513 85.582 1.00 47.40 . 4 2733 HETA O O HOH . 42 . −3.006 −22.530 47.973 1.00 45.26 . 4 2734 HETA O O HOH . 43 . 7.170 −1.009 77.408 1.00 33.27 . 4 2735 HETA O O HOH . 44 . 10.814 3.008 67.953 1.00 37.38 . 4 2736 HETA O O HOH . 45 . 8.757 −17.726 78.839 1.00 41.19 . 4 2737 HETA O O HOH . 46 . 16.517 4.841 44.813 1.00 44.24 . 4 2738 HETA O O HOH . 47 . −4.009 6.791 60.053 1.00 36.70 . 4 2739 HETA O O HOH . 48 . 11.433 4.110 43.449 1.00 42.44 . 4 2740 HETA O O HOH . 49 . 26.897 −3.874 81.674 1.00 48.43 . 4 2741 HETA O O HOH . 50 . 32.408 8.501 60.143 1.00 43.94 . 4 2742 HETA O O HOH . 51 . 14.752 4.244 55.820 1.00 37.21 . 4 2743 HETA O O HOH . 52 . −6.599 −6.716 60.928 1.00 38.22 . 4 2744 HETA O O HOH . 53 . 1.098 −16.701 76.721 1.00 43.82 . 4 2745 HETA O O HOH . 54 . 24.560 −20.006 49.768 1.00 41.45 . 4 2746 HETA O O HOH . 55 . −8.356 −1.073 59.999 1.00 36.39 . 4 2747 HETA O O HOH . 56 . −20.296 −0.174 52.977 1.00 48.02 . 4 2748 HETA O O HOH . 57 . 7.650 3.740 43.152 1.00 43.96 . 4 2749 HETA O O HOH . 58 . −1.956 −22.751 41.418 1.00 33.98 . 4 2750 HETA O O HOH . 59 . 29.914 3.036 61.374 1.00 32.05 . 4 2751 HETA O O HOH . 60 . 26.465 −7.555 63.716 1.00 38.62 . 4 2752 HETA O O HOH . 61 . 11.196 4.936 54.878 1.00 44.90 . 4 2753 HETA O O HOH . 62 . −0.575 0.150 69.708 1.00 36.91 . 4 2754 HETA O O HOH . 63 . −5.154 −12.557 58.822 1.00 36.05 . 4 2755 HETA O O HOH . 64 . 8.622 −12.996 34.242 1.00 39.11 . 4 2756 HETA O O HOH . 65 . 39.418 8.023 57.709 1.00 44.06 . 4 2757 HETA O O HOH . 66 . 26.234 −13.973 81.675 1.00 46.56 . 4 2758 HETA O O HOH . 67 . 21.893 −21.031 90.256 1.00 43.69 . 4 2759 HETA O O HOH . 68 . −16.877 −14.663 34.885 1.00 46.76 . 4 2760 HETA O O HOH . 69 . 2.064 −2.708 77.539 1.00 49.04 . 4 2761 HETA O O HOH . 70 . 4.716 −15.964 69.075 1.00 41.83 . 4 2762 HETA O O HOH . 71 . −12.695 −14.602 33.417 1.00 38.87 . 4 2763 HETA O O HOH . 72 . 0.288 −14.476 28.995 1.00 44.99 . 4 2764 HETA O O HOH . 73 . −2.522 −16.335 64.493 1.00 40.68 . 4 2765 HETA O O HOH . 74 . 15.837 −7.587 45.299 1.00 29.04 . 4 2766 HETA O O HOH . 75 . 3.147 4.773 54.348 1.00 34.36 . 4 2767 HETA O O HOH . 76 . −17.628 −9.032 58.022 1.00 40.01 . 4 2768 HETA O O HOH . 77 . 15.182 −6.121 89.661 1.00 45.48 . 4 2769 HETA O O HOH . 78 . 14.125 4.345 43.112 1.00 43.24 . 4 2770 HETA O O HOH . 79 . 17.741 −0.041 35.945 1.00 49.99 . 4 2771 HETA O O HOH . 80 . 8.176 −3.602 86.520 1.00 45.04 . 4 2772 HETA O O HOH . 81 . 14.748 −12.679 89.298 1.00 46.01 . 4 2773 HETA O O HOH . 82 . −22.466 −16.394 53.560 1.00 39.25 . 4 2774 HETA O O HOH . 83 . 6.361 −5.784 34.167 1.00 49.12 . 4 2775 HETA O O HOH . 84 . 15.230 6.286 89.069 1.00 41.71 . 4 2776 HETA O O HOH . 85 . −2.701 −12.258 64.560 1.00 47.53 . 4 2777 HETA O O HOH . 86 . −20.329 −19.580 50.295 1.00 34.86 . 4 2778 HETA O O HOH . 87 . 16.001 3.526 75.008 1.00 38.29 . 4 2779 HETA O O HOH . 88 . 13.260 1.972 79.219 1.00 45.37 . 4 2780 HETA O O HOH . 89 . 7.497 −7.666 35.856 1.00 45.71 . 4 2781 HETA O O HOH . 90 . −12.603 −20.367 37.600 1.00 52.44 . 4 2782 HETA O O HOH . 91 . −4.424 −19.719 50.862 1.00 42.86 . 4 2783 HETA O O HOH . 92 . −15.614 −19.392 61.942 1.00 45.41 . 4 2784 HETA O O HOH . 93 . −11.193 −7.642 28.159 1.00 47.53 . 4 2785 HETA O O HOH . 94 . 9.437 2.159 76.203 1.00 39.31 . 4 2786 HETA O O HOH . 95 . −22.022 −8.828 51.912 1.00 37.61 . 4 2787 HETA O O HOH . 96 . 5.561 −9.077 83.153 1.00 35.24 . 4 2788 HETA O O HOH . 97 . −21.679 −12.123 48.406 1.00 42.94 . 4 2789 HETA O O HOH . 98 . −2.237 4.535 33.252 1.00 47.22 . 4 2790 HETA O O HOH . 99 . −11.157 −11.475 59.206 1.00 47.30 . 4 2791 HETA O O HOH . 100 . 40.237 6.104 53.873 1.00 44.09 . 4 2792 HETA O O HOH . 101 . −5.938 −17.452 53.602 1.00 43.32 . 4 2793 HETA O O HOH . 102 . −6.860 −17.053 57.220 1.00 38.28 . 4 2794 HETA O O HOH . 103 . 18.390 −6.822 86.891 1.00 51.53 . 4 2795 HETA O O HOH . 104 . −7.508 −7.592 28.305 1.00 40.28 . 4 2796 HETA O O HOH . 105 . 20.844 4.841 48.597 1.00 51.40 . 4 2797 HETA O O HOH . 106 . 0.007 6.826 51.997 1.00 49.86 . 4 2798 HETA O O HOH . 107 . 17.763 −1.331 63.808 1.00 40.38 . 4 2799 HETA O O HOH . 108 . −18.190 −16.655 60.379 1.00 49.70 . 4 2800 HETA O O HOH . 109 . 12.519 −9.164 41.373 1.00 48.45 . 4 2801 HETA O O HOH . 110 . 22.941 3.338 100.433 1.00 51.34 . 4 2802 HETA O O HOH . 111 . 25.250 −6.443 79.872 1.00 43.51 . 4 2803 HETA O O HOH . 112 . −18.416 −22.508 53.996 1.00 42.86 . 4 2804 HETA O O HOH . 113 . 18.854 0.425 65.583 1.00 39.11 . 4 2805 HETA O O HOH . 1001 . −5.309 −14.988 56.675 1.00 41.76 . 4 2806 HETA O O HOH . 1002 . 0.054 −19.552 44.559 1.00 33.73 . 4 2807 HETA O O HOH . 1003 . 6.177 −5.294 86.321 1.00 43.80 . 4 2808 HETA O O HOH . 1004 . −7.139 5.791 49.300 1.00 48.57 . 4 2809 HETA O O HOH . 1005 . 3.997 −9.826 50.182 1.00 37.26 . 4 2810 HETA O O HOH . 1007 . 39.570 8.242 55.141 1.00 53.69 . 4 2811 HETA O O HOH . 1008 . 8.123 2.949 48.961 1.00 48.37 . 4 2812 HETA O O HOH . 1009 . −6.897 −12.617 61.178 1.00 47.36 . 4 2813 HETA O O HOH . 1010 . 17.731 0.913 56.857 1.00 49.69 . 4 2814 HETA O O HOH . 1011 . 8.650 4.467 39.307 1.00 49.64 . 4 2815 HETA O O HOH . 1012 . 40.440 9.085 59.684 1.00 54.25 . 4 2816 HETA O O HOH . 1013 . 5.358 −18.723 37.206 1.00 47.50 . 4 2817 HETA O O HOH . 1014 . 2.695 3.080 69.202 1.00 48.28 . 4 2818 HETA O O HOH . 1015 . −7.789 −8.857 61.880 1.00 37.96 . 4 2819 HETA O O HOH . 1016 . −8.725 −0.597 62.720 1.00 42.69 . 4 2820 HETA O O HOH . 1017 . −3.112 −15.577 55.825 1.00 44.53 . 4 2821 HETA O O HOH . 1018 . −17.325 0.162 41.186 1.00 51.16 . 4 2822 HETA O O HOH . 1019 . −16.012 −15.144 61.681 1.00 53.33 . 4 2823 HETA O O HOH . 1020 . −8.618 −4.846 61.487 1.00 48.42 . 4 2824 HETA O O HOH . 1021 . −17.371 −23.178 44.197 1.00 51.12 . 4 2825 HETA O O HOH . 1022 . 18.384 4.861 76.282 1.00 55.67 . 4 2826 HETA O O HOH . 1023 . 26.500 −21.372 50.516 1.00 45.52 . 4 2827 HETA O O HOH . 1024 . 6.076 −2.453 79.620 1.00 46.76 . 4 2828 HETA O O HOH . 1025 . 7.043 −14.324 31.575 1.00 45.13 . 4 2829 HETA O O HOH . 1026 . 4.713 6.009 43.639 1.00 60.96 . 4 2830 HETA O O HOH . 1027 . −21.690 −18.044 41.967 1.00 54.13 . 4 2831 HETA O O HOH . 1028 . 7.479 −23.701 51.344 1.00 61.04 . 4 2832 HETA O O HOH . 1029 . 20.325 4.960 79.627 1.00 56.05 . 4 2833 HETA O O HOH . 1030 . 17.620 2.965 64.955 1.00 52.21 . 4 2834 HETA O O HOH . 1031 . −0.681 −13.183 68.153 1.00 50.52 . 4 2835 HETA O O HOH . 1032 . −14.908 −0.016 29.970 1.00 53.53 . 4 2836 HETA O O HOH . 1033 . 9.221 4.899 76.035 1.00 42.65 . 4 2837 HETA O O HOH . 1034 . 0.521 6.183 40.387 1.00 49.43 . 4 2838 HETA O O HOH . 1035 . −9.657 −3.375 59.781 1.00 49.88 . 4 2839 HETA O O HOH . 1036 . 8.992 1.359 47.197 1.00 43.54 . 4 2840 HETA O O HOH . 1037 . 4.960 −14.839 73.712 1.00 47.91 . 4 2841 HETA O O HOH . 1038 . −6.492 −10.409 57.807 1.00 39.36 . 4 2842 HETA O O HOH . 1039 . −20.730 −6.102 39.507 1.00 55.97 . 4 2843 HETA O O HOH . 1040 . 15.910 0.416 62.415 1.00 51.07 . 4 2844 HETA O O HOH . 1041 . −18.362 −22.673 47.871 1.00 51.55 . 4 2845 HETA O O HOH . 1042 . −3.862 −18.407 63.376 1.00 50.62 . 4 2846 HETA O O HOH . 1043 . 9.614 5.251 41.701 1.00 45.87 . 4 2847 HETA O O HOH . 1044 . 12.105 −15.013 91.048 1.00 49.41 . 4 2848 HETA O O HOH . 1045 . 17.559 −15.967 88.843 1.00 52.13 . 4 2849 HETA O O HOH . 1046 . 23.442 −2.294 60.885 1.00 50.95 . 4 2850 HETA O O HOH . 1047 . −2.644 −11.978 67.257 1.00 49.38 . 4 2851 HETA O O HOH . 1048 . −0.673 2.886 32.051 1.00 56.75 . 4 2852 HETA O O HOH . 1049 . −14.776 −0.562 41.070 1.00 49.77 . 4 2853 HETA O O HOH . 1050 . 15.824 3.715 36.807 1.00 52.56 . 4 2854 HETA O O HOH . 1051 . −3.000 4.807 30.441 1.00 65.46 . 4 2855 HETA O O HOH . 1052 . 3.882 −12.386 62.395 1.00 44.66 . 4 2856 HETA O O HOH . 1053 . 19.032 −4.967 88.493 1.00 57.91 . 4 2857 HETA O O HOH . 1054 . −2.684 0.419 32.367 1.00 54.57 . 4 2858 HETA O O HOH . 1055 . 19.409 −24.166 32.750 1.00 62.33 . 4 2859 HETA O O HOH . 1056 . 6.897 −16.979 80.968 1.00 48.63 . 4 2860 HETA O O HOH . 1057 . −13.220 −5.741 61.740 1.00 58.42 . 4 2861 HETA O O HOH . 1058 . −0.529 −28.072 60.340 1.00 58.04 . 4 2862 HETA O O HOH . 1059 . 12.301 −10.714 39.000 1.00 47.31 . 4 2863 HETA O O HOH . 1060 . 5.914 3.247 33.885 1.00 61.47 . 4 2864 HETA O O HOH . 1061 . −3.439 −22.301 50.418 1.00 48.48 . 4 2865 HETA O O HOH . 1062 . 11.859 −16.071 41.204 1.00 53.27 . 4 2866 HETA O O HOH . 1063 . −19.001 −18.326 62.689 1.00 48.05 . 4 2867 HETA O O HOH . 1064 . −12.776 −23.170 35.816 1.00 49.63 . 4 2868 HETA O O HOH . 1065 . −18.198 −11.539 57.047 1.00 44.15 . 4 2869 HETA O O HOH . 1066 . 1.482 −20.767 67.741 1.00 54.20 . 4 2870 HETA O O HOH . 1067 . −20.273 −8.309 57.847 1.00 59.37 . 4 2871 HETA O O HOH . 1068 . −0.725 −9.033 26.268 1.00 64.09 . 4 2872 HETA O O HOH . 1069 . 3.631 −19.826 41.838 1.00 57.93 . 4 2873 HETA O O HOH . 1070 . −0.009 −8.274 50.402 1.00 38.42 . 4 2874 HETA O O HOH . 1071 . 5.978 −16.403 71.385 1.00 49.25 . 4 2875 HETA O O HOH . 1072 . 7.757 −19.740 69.379 1.00 53.15 . 4 2876 HETA O O HOH . 1073 . 3.002 −17.524 74.082 1.00 63.37 . 4 2877 HETA O O HOH . 1074 . 9.782 −20.058 78.442 1.00 50.32 . 4 2878 HETA O O HOH . 1075 . −9.059 −25.196 35.316 1.00 54.87 . 4 2879 HETA O O HOH . 1076 . −18.474 −8.410 32.456 1.00 64.19 . 4 2880 HETA O O HOH . 1077 . 4.136 −11.258 83.059 1.00 53.91 . 4 2881 HETA O O HOH . 1078 . 11.178 −7.235 39.592 1.00 56.00 . 4 2882 HETA O O HOH . 1079 . −8.527 −28.223 41.713 1.00 54.36 . 4 2883 HETA O O HOH . 1080 . −15.712 −20.987 39.112 1.00 46.14 . 4 2884 HETA O O HOH . 1081 . −22.469 −7.361 54.182 1.00 55.47 . 4 2885 HETA O O HOH . 1082 . −19.494 −14.494 59.674 1.00 46.78 . 4 2886 HETA O O HOH . 1083 . 13.094 6.637 46.356 1.00 53.22 . 4 2887 HETA O O HOH . 1084 . −8.405 −10.759 59.829 1.00 57.59 . 4 2888 HETA O O HOH . 1085 . −18.571 0.927 58.155 1.00 53.04 . 4 2889 HETA O O HOH . 1086 . −15.645 −25.385 54.165 1.00 47.28 . 4 2890 HETA O O HOH . 1087 . −10.667 1.257 53.747 1.00 50.60 . 4 2891 HETA O O HOH . 1088 . 12.921 6.620 51.991 1.00 47.75 . 4 2892 HETA O O HOH . 1089 . −12.062 −17.707 30.020 1.00 51.36 . 4 2893 HETA O O HOH . 1090 . −4.655 −9.930 27.132 1.00 50.91 . 4 2894 HETA O O HOH . 1091 . 2.997 −7.477 85.762 1.00 56.08 . 4 2895 HETA O O HOH . 1092 . 11.980 −20.693 67.090 1.00 46.64 . 4 2896 HETA O O HOH . 1093 . −23.449 −6.324 42.122 1.00 60.53 . 4 2897 HETA O O HOH . 1094 . −13.984 1.405 39.444 1.00 45.62 . 4 2898 HETA O O HOH . 1095 . 0.725 −0.820 72.375 1.00 58.19 . 4 2899 HETA O O HOH . 1096 . −3.200 8.070 43.480 1.00 57.84 . 4 2900 HETA O O HOH . 1097 . −2.057 −18.386 52.377 1.00 68.38 . 4 2901 HETA O O HOH . 1098 . −15.703 −8.025 28.921 1.00 56.15 . 4 2902 HETA O O HOH . 1099 . 4.155 4.144 37.209 1.00 59.68 . 4 2903 HETA O O HOH . 1100 . 30.384 −21.406 44.868 1.00 57.20 . 4 2904 HETA O O HOH . 1101 . −15.484 −11.801 62.783 1.00 62.20 . 4 2905

APPENDIX D ATOM TYPE RES # X Y Z OCC B ATOM ATOM N N ARG A 8 . −17.833 −8.192 54.153 1.00 41.12 . 1 1 ATOM C CA ARG A 8 . −16.596 −8.642 54.818 1.00 42.12 . 1 2 ATOM C C ARG A 8 . −16.535 −10.172 54.840 1.00 42.44 . 1 3 ATOM O O ARG A 8 . −17.367 −10.858 55.454 1.00 42.89 . 1 4 ATOM C CB ARG A 8 . −16.512 −8.081 56.223 1.00 41.84 . 1 5 ATOM C CG ARG A 8 . −15.112 −8.187 56.760 1.00 43.09 . 1 6 ATOM C CD ARG A 8 . −14.105 −7.703 55.729 1.00 40.76 . 1 7 ATOM N NE ARG A 8 . −12.766 −8.191 56.055 1.00 42.31 . 1 8 ATOM C CZ ARG A 8 . −11.637 −7.648 55.598 1.00 40.85 . 1 9 ATOM N NH1 ARG A 8 . −11.688 −6.590 54.796 1.00 41.39 . 1 10 ATOM N NH2 ARG A 8 . −10.455 −8.157 55.934 1.00 41.02 . 1 11 ATOM N N LYS A 9 . −15.511 −10.666 54.154 1.00 42.21 . 1 12 ATOM C CA LYS A 9 . −15.261 −12.073 53.928 1.00 40.40 . 1 13 ATOM C C LYS A 9 . −13.805 −12.367 54.337 1.00 39.99 . 1 14 ATOM O O LYS A 9 . −13.244 −11.661 55.176 1.00 38.93 . 1 15 ATOM C CB LYS A 9 . −15.464 −12.299 52.420 1.00 41.00 . 1 16 ATOM C CG LYS A 9 . −16.482 −11.335 51.782 1.00 39.58 . 1 17 ATOM C CD LYS A 9 . −17.632 −12.084 51.139 1.00 40.05 . 1 18 ATOM C CE LYS A 9 . −18.576 −11.149 50.431 1.00 39.65 . 1 19 ATOM N NZ LYS A 9 . −19.478 −11.910 49.523 1.00 40.51 . 1 20 ATOM N N PRO A 10 . −13.184 −13.424 53.765 1.00 39.96 . 1 21 ATOM C CA PRO A 10 . −11.784 −13.794 54.065 1.00 39.71 . 1 22 ATOM C C PRO A 10 . −10.831 −13.131 53.053 1.00 40.14 . 1 23 ATOM O O PRO A 10 . −11.080 −12.022 52.611 1.00 38.80 . 1 24 ATOM C CB PRO A 10 . −11.796 −15.302 53.892 1.00 40.08 . 1 25 ATOM C CG PRO A 10 . −12.712 −15.459 52.710 1.00 40.20 . 1 26 ATOM C CD PRO A 10 . −13.868 −14.553 53.097 1.00 39.98 . 1 27 ATOM N N SER A 11 . −9.758 −13.820 52.657 1.00 40.34 . 1 28 ATOM C CA SER A 11 . −8.821 −13.257 51.673 1.00 39.63 . 1 29 ATOM C C SER A 11 . −9.379 −13.135 50.233 1.00 38.30 . 1 30 ATOM O O SER A 11 . −8.631 −13.047 49.244 1.00 38.05 . 1 31 ATOM C CB SER A 11 . −7.526 −14.072 51.645 1.00 41.79 . 1 32 ATOM O OG SER A 11 . −6.609 −13.554 50.683 1.00 43.17 . 1 33 ATOM N N GLU A 12 . −10.696 −13.159 50.097 1.00 36.97 . 1 34 ATOM C CA GLU A 12 . −11.292 −12.962 48.780 1.00 34.97 . 1 35 ATOM C C GLU A 12 . −11.368 −11.430 48.635 1.00 31.92 . 1 36 ATOM O O GLU A 12 . −11.714 −10.901 47.587 1.00 31.99 . 1 37 ATOM C CB GLU A 12 . −12.685 −13.589 48.691 1.00 37.87 . 1 38 ATOM C CG GLU A 12 . −13.380 −13.727 50.017 1.00 40.59 . 1 39 ATOM C CD GLU A 12 . −14.671 −14.567 49.930 1.00 42.99 . 1 40 ATOM O OE1 GLU A 12 . −15.264 −14.860 50.996 1.00 43.90 . 1 41 ATOM O OE2 GLU A 12 . −15.093 −14.931 48.800 1.00 44.16 . 1 42 ATOM N N ILE A 13 . −11.033 −10.735 49.711 1.00 29.40 . 1 43 ATOM C CA ILE A 13 . −10.982 −9.287 49.687 1.00 27.60 . 1 44 ATOM C C ILE A 13 . −9.796 −8.847 48.807 1.00 26.39 . 1 45 ATOM O O ILE A 13 . −9.922 −7.920 48.022 1.00 23.73 . 1 46 ATOM C CB ILE A 13 . −10.800 −8.715 51.096 1.00 27.22 . 1 47 ATOM C CG1 ILE A 13 . −12.078 −8.968 51.903 1.00 26.49 . 1 48 ATOM C CG2 ILE A 13 . −10.458 −7.200 51.039 1.00 27.93 . 1 49 ATOM C CD1 ILE A 13 . −13.359 −8.494 51.202 1.00 26.62 . 1 50 ATOM N N PHE A 14 . −8.639 −9.486 48.971 1.00 25.60 . 1 51 ATOM C CA PHE A 14 . −7.457 −9.144 48.155 1.00 25.49 . 1 52 ATOM C C PHE A 14 . −7.797 −9.375 46.659 1.00 25.20 . 1 53 ATOM O O PHE A 14 . −7.435 −8.585 45.772 1.00 22.78 . 1 54 ATOM C CB PHE A 14 . −6.255 −9.993 48.629 1.00 25.79 . 1 55 ATOM C CG PHE A 14 . −4.935 −9.713 47.912 1.00 26.00 . 1 56 ATOM C CD1 PHE A 14 . −4.638 −8.466 47.364 1.00 26.63 . 1 57 ATOM C CD2 PHE A 14 . −3.971 −10.709 47.852 1.00 25.35 . 1 58 ATOM C CE1 PHE A 14 . −3.399 −8.224 46.768 1.00 26.99 . 1 59 ATOM C CE2 PHE A 14 . −2.722 −10.468 47.253 1.00 27.29 . 1 60 ATOM C CZ PHE A 14 . −2.445 −9.228 46.713 1.00 26.15 . 1 61 ATOM N N LYS A 15 . −8.515 −10.444 46.364 1.00 23.85 . 1 62 ATOM C CA LYS A 15 . −8.877 −10.678 44.968 1.00 24.22 . 1 63 ATOM C C LYS A 15 . −9.807 −9.576 44.394 1.00 24.18 . 1 64 ATOM O O LYS A 15 . −9.687 −9.160 43.238 1.00 21.98 . 1 65 ATOM C CB LYS A 15 . −9.558 −12.027 44.877 1.00 27.81 . 1 66 ATOM C CG LYS A 15 . −10.075 −12.398 43.499 1.00 30.65 . 1 67 ATOM C CD LYS A 15 . −10.808 −13.761 43.615 1.00 33.75 . 1 68 ATOM C CE LYS A 15 . −11.292 −14.285 42.261 1.00 34.30 . 1 69 ATOM N NZ LYS A 15 . −11.856 −13.209 41.361 1.00 37.08 . 1 70 ATOM N N ALA A 16 . −10.764 −9.142 45.212 1.00 21.02 . 1 71 ATOM C CA ALA A 16 . −11.711 −8.096 44.810 1.00 19.71 . 1 72 ATOM C C ALA A 16 . −10.968 −6.759 44.683 1.00 16.90 . 1 73 ATOM O O ALA A 16 . −11.316 −5.925 43.849 1.00 14.68 . 1 74 ATOM C CB ALA A 16 . −12.829 −7.985 45.883 1.00 19.44 . 1 75 ATOM N N GLN A 17 . −9.966 −6.573 45.548 1.00 17.19 . 1 76 ATOM C CA GLN A 17 . −9.173 −5.365 45.475 1.00 16.27 . 1 77 ATOM C C GLN A 17 . −8.418 −5.359 44.133 1.00 16.87 . 1 78 ATOM O O GLN A 17 . −8.330 −4.343 43.463 1.00 15.11 . 1 79 ATOM C CB GLN A 17 . −8.176 −5.288 46.665 1.00 17.39 . 1 80 ATOM C CG GLN A 17 . −7.333 −3.970 46.573 1.00 20.19 . 1 81 ATOM C CD GLN A 17 . −6.468 −3.678 47.771 1.00 21.79 . 1 82 ATOM O OE1 GLN A 17 . −6.155 −4.577 48.552 1.00 23.15 . 1 83 ATOM N NE2 GLN A 17 . −6.061 −2.399 47.919 1.00 20.05 . 1 84 ATOM N N ALA A 18 . −7.868 −6.494 43.721 1.00 16.03 . 1 85 ATOM C CA ALA A 18 . −7.164 −6.542 42.438 1.00 16.73 . 1 86 ATOM C C ALA A 18 . −8.103 −6.171 41.258 1.00 16.01 . 1 87 ATOM O O ALA A 18 . −7.736 −5.354 40.360 1.00 15.84 . 1 88 ATOM C CB ALA A 18 . −6.556 −7.945 42.246 1.00 17.52 . 1 89 ATOM N N LEU A 19 . −9.341 −6.687 41.310 1.00 15.46 . 1 90 ATOM C CA LEU A 19 . −10.318 −6.342 40.292 1.00 16.22 . 1 91 ATOM C C LEU A 19 . −10.629 −4.836 40.293 1.00 16.69 . 1 92 ATOM O O LEU A 19 . −10.652 −4.180 39.250 1.00 15.74 . 1 93 ATOM C CB LEU A 19 . −11.631 −7.099 40.532 1.00 18.69 . 1 94 ATOM C CG LEU A 19 . −12.720 −6.760 39.497 1.00 18.01 . 1 95 ATOM C CD1 LEU A 19 . −12.272 −7.172 38.114 1.00 19.80 . 1 96 ATOM C CD2 LEU A 19 . −14.021 −7.535 39.865 1.00 22.78 . 1 97 ATOM N N LEU A 20 . −10.909 −4.272 41.483 1.00 13.96 . 1 98 ATOM C CA LEU A 20 . −11.206 −2.851 41.569 1.00 15.25 . 1 99 ATOM C C LEU A 20 . −10.030 −2.039 40.989 1.00 15.35 . 1 100 ATOM O O LEU A 20 . −10.250 −1.132 40.198 1.00 14.39 . 1 101 ATOM C CB LEU A 20 . −11.448 −2.426 43.030 1.00 16.53 . 1 102 ATOM C CG LEU A 20 . −11.671 −0.900 43.249 1.00 17.90 . 1 103 ATOM C CD1 LEU A 20 . −12.949 −0.417 42.570 1.00 19.83 . 1 104 ATOM C CD2 LEU A 20 . −11.790 −0.606 44.767 1.00 18.35 . 1 105 ATOM N N TYR A 21 . −8.792 −2.362 41.370 1.00 14.75 . 1 106 ATOM C CA TYR A 21 . −7.648 −1.601 40.852 1.00 16.31 . 1 107 ATOM C C TYR A 21 . −7.493 −1.696 39.335 1.00 15.62 . 1 108 ATOM O O TYR A 21 . −7.120 −0.712 38.680 1.00 15.30 . 1 109 ATOM C CB TYR A 21 . −6.372 −2.098 41.521 1.00 16.42 . 1 110 ATOM C CG TYR A 21 . −6.118 −1.551 42.892 1.00 19.05 . 1 111 ATOM C CD1 TYR A 21 . −7.141 −1.027 43.683 1.00 20.47 . 1 112 ATOM C CD2 TYR A 21 . −4.828 −1.572 43.411 1.00 22.21 . 1 113 ATOM C CE1 TYR A 21 . −6.898 −0.549 44.965 1.00 22.72 . 1 114 ATOM C CE2 TYR A 21 . −4.567 −1.081 44.698 1.00 23.36 . 1 115 ATOM C CZ TYR A 21 . −5.603 −0.577 45.459 1.00 22.68 . 1 116 ATOM O OH TYR A 21 . −5.325 −0.065 46.722 1.00 25.01 . 1 117 ATOM N N LYS A 22 . −7.774 −2.866 38.790 1.00 15.66 . 1 118 ATOM C CA LYS A 22 . −7.679 −3.052 37.366 1.00 17.58 . 1 119 ATOM C C LYS A 22 . −8.593 −2.041 36.695 1.00 16.66 . 1 120 ATOM O O LYS A 22 . −8.256 −1.446 35.675 1.00 17.27 . 1 121 ATOM C CB LYS A 22 . −8.133 −4.452 36.996 1.00 18.01 . 1 122 ATOM C CG LYS A 22 . −8.172 −4.755 35.483 1.00 21.28 . 1 123 ATOM C CD LYS A 22 . −8.414 −6.249 35.231 1.00 26.46 . 1 124 ATOM C CE LYS A 22 . −8.424 −6.563 33.709 1.00 30.64 . 1 125 ATOM N NZ LYS A 22 . −8.588 −8.056 33.405 1.00 34.74 . 1 126 ATOM N N HIS A 23 . −9.782 −1.824 37.285 1.00 15.47 . 1 127 ATOM C CA HIS A 23 . −10.705 −0.907 36.662 1.00 14.26 . 1 128 ATOM C C HIS A 23 . −10.488 0.554 36.946 1.00 14.30 . 1 129 ATOM O O HIS A 23 . −10.708 1.434 36.113 1.00 13.55 . 1 130 ATOM C CB HIS A 23 . −12.131 −1.345 36.999 1.00 15.66 . 1 131 ATOM C CG HIS A 23 . −12.547 −2.523 36.200 1.00 15.79 . 1 132 ATOM N ND1 HIS A 23 . −12.231 −3.821 36.550 1.00 19.04 . 1 133 ATOM C CD2 HIS A 23 . −13.138 −2.587 34.986 1.00 15.08 . 1 134 ATOM C CE1 HIS A 23 . −12.602 −4.642 35.570 1.00 18.72 . 1 135 ATOM N NE2 HIS A 23 . −13.151 −3.913 34.616 1.00 18.57 . 1 136 ATOM N N ILE A 24 . −10.037 0.856 38.158 1.00 14.04 . 1 137 ATOM C CA ILE A 24 . −9.726 2.241 38.453 1.00 14.13 . 1 138 ATOM C C ILE A 24 . −8.658 2.728 37.468 1.00 14.89 . 1 139 ATOM O O ILE A 24 . −8.777 3.844 36.950 1.00 14.66 . 1 140 ATOM C CB ILE A 24 . −9.116 2.373 39.904 1.00 14.59 . 1 141 ATOM C CG1 ILE A 24 . −10.224 2.238 40.955 1.00 15.43 . 1 142 ATOM C CG2 ILE A 24 . −8.408 3.735 40.051 1.00 14.87 . 1 143 ATOM C CD1 ILE A 24 . −9.625 2.208 42.401 1.00 15.15 . 1 144 ATOM N N TYR A 25 . −7.673 1.875 37.189 1.00 15.26 . 1 145 ATOM C CA TYR A 25 . −6.557 2.318 36.333 1.00 15.08 . 1 146 ATOM C C TYR A 25 . −6.663 1.873 34.876 1.00 14.79 . 1 147 ATOM O O TYR A 25 . −5.681 1.938 34.128 1.00 15.15 . 1 148 ATOM C CB TYR A 25 . −5.251 1.797 36.980 1.00 15.49 . 1 149 ATOM C CG TYR A 25 . −4.946 2.432 38.310 1.00 16.20 . 1 150 ATOM C CD1 TYR A 25 . −5.150 1.743 39.500. 1.00 18.49 . 1 151 ATOM C CD2 TYR A 25 . −4.430 3.731 38.374 1.00 17.13 . 1 152 ATOM C CE1 TYR A 25 . −4.826 2.383 40.756 1.00 18.64 . 1 153 ATOM C CE2 TYR A 25 . −4.094 4.359 39.589 1.00 18.58 . 1 154 ATOM C CZ TYR A 25 . −4.304 3.670 40.767 1.00 19.38 . 1 155 ATOM O OH TYR A 25 . −3.973 4.310 41.955 1.00 20.85 . 1 156 ATOM N N ALA A 26 . −7.829 1.379 34.462 1.00 13.41 . 1 157 ATOM C CA ALA A 26 . −7.998 0.931 33.077 1.00 13.44 . 1 158 ATOM C C ALA A 26 . −7.651 2.013 32.042 1.00 13.30 . 1 159 ATOM O O ALA A 26 . −7.208 1.651 30.941 1.00 13.52 . 1 160 ATOM C CB ALA A 26 . −9.472 0.402 32.861 1.00 13.24 . 1 161 ATOM N N PHE A 27 . −7.802 3.316 32.342 1.00 12.95 . 1 162 ATOM C CA PHE A 27 . −7.497 4.384 31.406 1.00 13.88 . 1 163 ATOM C C PHE A 27 . −6.036 4.302 30.985 1.00 14.37 . 1 164 ATOM O O PHE A 27 . −5.700 4.786 29.922 1.00 14.72 . 1 165 ATOM C CB PHE A 27 . −7.843 5.753 32.007 1.00 15.05 . 1 166 ATOM C CG PHE A 27 . −6.981 6.148 33.202 1.00 16.37 . 1 167 ATOM C CD1 PHE A 27 . −5.798 6.823 33.024 1.00 16.23 . 1 168 ATOM C CD2 PHE A 27 . −7.373 5.811 34.498 1.00 14.42 . 1 169 ATOM C CE1 PHE A 27 . −4.972 7.175 34.136 1.00 16.53 . 1 170 ATOM C CE2 PHE A 27 . −6.545 6.155 35.602 1.00 17.25 . 1 171 ATOM C CZ PHE A 27 . −5.349 6.833 35.396 1.00 16.99 . 1 172 ATOM N N ILE A 28 . −5.176 3.716 31.831 1.00 14.32 . 1 173 ATOM C CA ILE A 28 . −3.759 3.582 31.431 1.00 14.44 . 1 174 ATOM C C ILE A 28 . −3.589 2.686 30.213 1.00 13.89 . 1 175 ATOM O O ILE A 28 . −2.634 2.881 29.441 1.00 13.73 . 1 176 ATOM C CB ILE A 28 . −2.904 3.029 32.625 1.00 14.26 . 1 177 ATOM C CG1 ILE A 28 . −2.842 4.126 33.672 1.00 17.63 . 1 178 ATOM C CG2 ILE A 28 . −1.485 2.759 32.195 1.00 15.64 . 1 179 ATOM C CD1 ILE A 28 . −2.119 3.764 35.017 1.00 19.44 . 1 180 ATOM N N ASP A 29 . −4.494 1.728 30.011 1.00 13.55 . 1 181 ATOM C CA ASP A 29 . −4.450 0.874 28.803 1.00 14.55 . 1 182 ATOM C C ASP A 29 . −4.658 1.797 27.577 1.00 14.89 . 1 183 ATOM O O ASP A 29 . −3.927 1.713 26.566 1.00 14.50 . 1 184 ATOM C CB ASP A 29 . −5.555 −0.197 28.790 1.00 15.10 . 1 185 ATOM C CG ASP A 29 . −5.161 −1.511 29.510 1.00 19.75 . 1 186 ATOM O OD1 ASP A 29 . −3.955 −1.723 29.829 1.00 19.14 . 1 187 ATOM O OD2 ASP A 29 . −6.086 −2.323 29.717 1.00 19.25 . 1 188 ATOM N N SER A 30 . −5.598 2.731 27.674 1.00 13.53 . 1 189 ATOM C CA SER A 30 . −5.865 3.652 26.556 1.00 12.69 . 1 190 ATOM C C SER A 30 . −4.714 4.649 26.372 1.00 11.65 . 1 191 ATOM O O SER A 30 . −4.257 4.886 25.242 1.00 12.00 . 1 192 ATOM C CB SER A 30 . −7.159 4.449 26.796 1.00 13.88 . 1 193 ATOM O OG SER A 30 . −8.264 3.561 26.828 1.00 13.81 . 1 194 ATOM N N MET A 31 . −4.175 5.180 27.481 1.00 11.01 . 1 195 ATOM C CA MET A 31 . −3.158 6.204 27.359 1.00 11.73 . 1 196 ATOM C C MET A 31 . −1.809 5.637 26.916 1.00 11.31 . 1 197 ATOM O O MET A 31 . −1.034 6.297 26.232 1.00 12.13 . 1 198 ATOM C CB MET A 31 . −2.990 6.975 28.676 1.00 12.81 . 1 199 ATOM C CG MET A 31 . −4.197 7.764 29.073 1.00 12.25 . 1 200 ATOM S SD MET A 31 . −4.648 8.999 27.835 1.00 13.14 . 1 201 ATOM C CE MET A 31 . −5.933 8.101 26.775 1.00 14.16 . 1 202 ATOM N N SER A 32 . −1.547 4.400 27.313 1.00 11.82 . 1 203 ATOM C CA SER A 32 . −0.280 3.814 26.876 1.00 13.05 . 1 204 ATOM C C SER A 32 . −0.314 3.482 25.361 1.00 13.53 . 1 205 ATOM O O SER A 32 . 0.713 3.585 24.656 1.00 12.89 . 1 206 ATOM C CB SER A 32 . 0.101 2.559 27.715 1.00 14.63 . 1 207 ATOM O OG SER A 32 . −0.860 1.499 27.545 1.00 15.38 . 1 208 ATOM N N LEU A 33 . −1.494 3.132 24.854 1.00 13.36 . 1 209 ATOM C CA LEU A 33 . −1.664 2.818 23.437 1.00 12.78 . 1 210 ATOM C C LEU A 33 . −1.527 4.118 22.677 1.00 13.64 . 1 211 ATOM O O LEU A 33 . −0.818 4.158 21.648 1.00 11.72 . 1 212 ATOM C CB LEU A 33 . −3.028 2.204 23.202 1.00 13.41 . 1 213 ATOM C CG LEU A 33 . −3.455 2.009 21.749 1.00 12.81 . 1 214 ATOM C CD1 LEU A 33 . −2.535 1.026 21.078 1.00 14.94 . 1 215 ATOM C CD2 LEU A 33 . −4.930 1.508 21.690 1.00 14.63 . 1 216 ATOM N N LYS A 34 . −2.175 5.187 23.145 1.00 12.79 . 1 217 ATOM C CA LYS A 34 . −2.016 6.512 22.541 1.00 11.85 . 1 218 ATOM C C LYS A 34 . −0.538 6.922 22.504 1.00 12.60 . 1 219 ATOM O O LYS A 34 . −0.062 7.428 21.485 1.00 13.14 . 1 220 ATOM C CB LYS A 34 . −2.797 7.551 23.330 1.00 13.01 . 1 221 ATOM C CG LYS A 34 . −2.533 8.978 22.930 1.00 13.17 . 1 222 ATOM C CD LYS A 34 . −3.473 9.920 23.681 1.00 12.61 . 1 223 ATOM C CE LYS A 34 . −3.084 11.347 23.468 1.00 12.07 . 1 224 ATOM N NZ LYS A 34 . −4.260 12.298 23.695 1.00 13.50 . 1 225 ATOM N N TRP A 35 . 0.192 6.663 23.601 1.00 12.49 . 1 226 ATOM C CA TRP A 35 . 1.588 7.001 23.645 1.00 12.75 . 1 227 ATOM C C TRP A 35 . 2.378 6.254 22.574 1.00 12.26 . 1 228 ATOM O O TRP A 35 . 3.215 6.815 21.874 1.00 13.45 . 1 229 ATOM C CB TRP A 35 . 2.118 6.660 25.060 1.00 10.89 . 1 230 ATOM C CG TRP A 35 . 3.630 6.806 25.169 1.00 11.45 . 1 231 ATOM C CD1 TRP A 35 . 4.338 7.935 25.400 1.00 12.60 . 1 232 ATOM C CD2 TRP A 35 . 4.575 5.728 25.078 1.00 10.92 . 1 233 ATOM N NE1 TRP A 35 . 5.704 7.625 25.476 1.00 11.95 . 1 234 ATOM C CE2 TRP A 35 . 5.868 6.290 25.283 1.00 12.14 . 1 235 ATOM C CE3 TRP A 35 . 4.461 4.361 24.845 1.00 12.98 . 1 236 ATOM C CZ2 TRP A 35 . 7.051 5.515 25.265 1.00 11.84 . 1 237 ATOM C CZ3 TRP A 35 . 5.631 3.585 24.818 1.00 12.87 . 1 238 ATOM C CH2 TRP A 35 . 6.902 4.166 25.026 1.00 14.17 . 1 239 ATOM N N ALA A 36 . 2.125 4.966 22.420 1.00 11.99 . 1 240 ATOM C CA ALA A 36 . 2.870 4.233 21.396 1.00 13.19 . 1 241 ATOM C C ALA A 36 . 2.634 4.804 19.977 1.00 12.27 . 1 242 ATOM O O ALA A 36 . 3.588 4.913 19.181 1.00 13.26 . 1 243 ATOM C CB ALA A 36 . 2.505 2.729 21.442 1.00 14.73 . 1 244 ATOM N N VAL A 37 . 1.408 5.168 19.640 1.00 12.48 . 1 245 ATOM C CA VAL A 37 . 1.100 5.744 18.348 1.00 12.87 . 1 246 ATOM C C VAL A 37 . 1.747 7.137 18.227 1.00 11.85 . 1 247 ATOM O O VAL A 37 . 2.411 7.430 17.184 1.00 13.74 . 1 248 ATOM C CB VAL A 37 . −0.429 5.853 18.172 1.00 11.39 . 1 249 ATOM C CG1 VAL A 37 . −0.746 6.746 16.964 1.00 13.67 . 1 250 ATOM C CG2 VAL A 37 . −0.981 4.456 17.996 1.00 12.71 . 1 251 ATOM N N GLU A 38 . 1.662 7.980 19.263 1.00 12.86 . 1 252 ATOM C CA GLU A 38 . 2.251 9.324 19.169 1.00 12.74 . 1 253 ATOM C C GLU A 38 . 3.760 9.277 19.045 1.00 13.27 . 1 254 ATOM O O GLU A 38 . 4.374 10.148 18.409 1.00 13.96 . 1 255 ATOM C CB GLU A 38 . 1.880 10.170 20.395 1.00 13.35 . 1 256 ATOM C CG GLU A 38 . 0.412 10.579 20.313 1.00 14.35 . 1 257 ATOM C CD GLU A 38 . 0.023 11.638 21.325 1.00 14.33 . 1 258 ATOM O OE1 GLU A 38 . 0.693 11.740 22.379 1.00 14.27 . 1 259 ATOM O OE2 GLU A 38 . −0.954 12.367 21.056 1.00 14.49 . 1 260 ATOM N N MET A 39 . 4.383 8.275 19.677 1.00 12.49 . 1 261 ATOM C CA MET A 39 . 5.836 8.128 19.560 1.00 13.38 . 1 262 ATOM C C MET A 39 . 6.233 7.483 18.245 1.00 14.27 . 1 263 ATOM O O MET A 39 . 7.432 7.350 17.973 1.00 15.67 . 1 264 ATOM C CB MET A 39 . 6.373 7.267 20.739 1.00 13.41 . 1 265 ATOM C CG MET A 39 . 6.099 7.840 22.094 1.00 15.98 . 1 266 ATOM S SD MET A 39 . 7.126 9.281 22.449 1.00 15.26 . 1 267 ATOM C CE MET A 39 . 8.809 8.431 22.610 1.00 16.48 . 1 268 ATOM N N ASN A 40 . 5.253 7.022 17.439 1.00 13.80 . 1 269 ATOM C CA ASN A 40 . 5.460 6.396 16.123 1.00 14.64 . 1 270 ATOM C C ASN A 40 . 6.192 5.072 16.221 1.00 14.85 . 1 271 ATOM O O ASN A 40 . 6.864 4.641 15.280 1.00 14.41 . 1 272 ATOM C CB ASN A 40 . 6.230 7.381 15.193 1.00 15.63 . 1 273 ATOM C CG ASN A 40 . 6.071 7.042 13.717 1.00 14.42 . 1 274 ATOM O OD1 ASN A 40 . 4.997 6.593 13.294 1.00 16.34 . 1 275 ATOM N ND2 ASN A 40 . 7.159 7.235 12.923 1.00 17.05 . 1 276 ATOM N N ILE A 41 . 5.998 4.376 17.333 1.00 14.59 . 1 277 ATOM C CA ILE A 41 . 6.711 3.123 17.513 1.00 13.41 . 1 278 ATOM C C ILE A 41 . 6.391 1.995 16.530 1.00 15.34 . 1 279 ATOM O O ILE A 41 . 7.306 1.359 15.998 1.00 14.22 . 1 280 ATOM C CB ILE A 41 . 6.647 2.740 19.006 1.00 13.92 . 1 281 ATOM C CG1 ILE A 41 . 7.469 3.773 19.796 1.00 12.79 . 1 282 ATOM C CG2 ILE A 41 . 7.187 1.316 19.226 1.00 14.30 . 1 283 ATOM C CD1 ILE A 41 . 7.303 3.593 21.340 1.00 14.37 . 1 284 ATOM N N PRO A 42 . 5.105 1.754 16.205 1.00 14.10 . 1 285 ATOM C CA PRO A 42 . 4.787 0.703 15.247 1.00 14.37 . 1 286 ATOM C C PRO A 42 . 5.529 0.959 13.904 1.00 15.04 . 1 287 ATOM O O PRO A 42 . 6.146 0.040 13.350 1.00 16.04 . 1 288 ATOM C CB PRO A 42 . 3.261 0.807 15.112 1.00 14.13 . 1 289 ATOM C CG PRO A 42 . 2.852 1.176 16.558 1.00 15.00 . 1 290 ATOM C CD PRO A 42 . 3.890 2.266 16.880 1.00 15.16 . 1 291 ATOM N N ASN A 43 . 5.509 2.195 13.403 1.00 15.15 . 1 292 ATOM C CA ASN A 43 . 6.185 2.443 12.131 1.00 15.98 . 1 293 ATOM C C ASN A 43 . 7.715 2.307 12.246 1.00 15.64 . 1 294 ATOM O O ASN A 43 . 8.345 1.784 11.308 1.00 15.75 . 1 295 ATOM C CB ASN A 43 . 5.814 3.826 11.604 1.00 16.86 . 1 296 ATOM C CG ASN A 43 . 4.359 3.890 11.129 1.00 18.06 . 1 297 ATOM O OD1 ASN A 43 . 3.909 2.991 10.525 1.00 19.94 . 1 298 ATOM N ND2 ASN A 43 . 3.673 4.987 11.374 1.00 18.83 . 1 299 ATOM N N ILE A 44 . 8.287 2.739 13.378 1.00 14.44 . 1 300 ATOM C CA ILE A 44 . 9.717 2.619 13.558 1.00 15.13 . 1 301 ATOM C C ILE A 44 . 10.081 1.147 13.483 1.00 15.39 . 1 302 ATOM O O ILE A 44 . 11.074 0.769 12.837 1.00 15.98 . 1 303 ATOM C CB ILE A 44 . 10.138 3.184 14.926 1.00 16.23 . 1 304 ATOM C CG1 ILE A 44 . 10.144 4.712 14.858 1.00 14.71 . 1 305 ATOM C CG2 ILE A 44 . 11.488 2.630 15.349 1.00 15.84 . 1 306 ATOM C CD1 ILE A 44 . 10.210 5.395 16.247 1.00 18.03 . 1 307 ATOM N N ILE A 45 . 9.297 0.285 14.134 1.00 16.23 . 1 308 ATOM C CA ILE A 45 . 9.628 −1.128 14.076 1.00 15.78 . 1 309 ATOM C C ILE A 45 . 9.457 −1.705 12.669 1.00 16.41 . 1 310 ATOM O O ILE A 45 . 10.330 −2.477 12.201 1.00 16.62 . 1 311 ATOM C CB ILE A 45 . 8.825 −1.917 15.122 1.00 15.54 . 1 312 ATOM C CG1 ILE A 45 . 9.254 −1.463 16.512 1.00 17.36 . 1 313 ATOM C CG2 ILE A 45 . 9.119 −3.416 14.972 1.00 17.47 . 1 314 ATOM C CD1 ILE A 45 . 8.415 −2.093 17.703 1.00 17.13 . 1 315 ATOM N N GLN A 46 . 8.371 −1.351 11.982 1.00 16.37 . 1 316 ATOM C CA GLN A 46 . 8.153 −1.818 10.627 1.00 16.72 . 1 317 ATOM C C GLN A 46 . 9.335 −1.413 9.728 1.00 17.55 . 1 318 ATOM O O GLN A 46 . 9.851 −2.240 8.951 1.00 19.40 . 1 319 ATOM C CB GLN A 46 . 6.840 −1.228 10.071 1.00 18.68 . 1 320 ATOM C CG GLN A 46 . 6.551 −1.512 8.588 1.00 20.75 . 1 321 ATOM C CD GLN A 46 . 6.323 −3.007 8.344 1.00 24.22 . 1 322 ATOM O OE1 GLN A 46 . 5.821 −3.704 9.218 1.00 26.15 . 1 323 ATOM N NE2 GLN A 46 . 6.702 −3.499 7.169 1.00 28.65 . 1 324 ATOM N N ASN A 47 . 9.758 −0.151 9.854 1.00 17.10 . 1 325 ATOM C CA ASN A 47 . 10.858 0.386 9.012 1.00 17.37 . 1 326 ATOM C C ASN A 47 . 12.172 −0.286 9.358 1.00 18.10 . 1 327 ATOM O O ASN A 47 . 13.050 −0.417 8.480 1.00 18.19 . 1 328 ATOM C CB ASN A 47 . 10.945 1.887 9.216 1.00 18.19 . 1 329 ATOM C CG ASN A 47 . 9.722 2.623 8.659 1.00 20.14 . 1 330 ATOM O OD1 ASN A 47 . 9.487 3.799 8.980 1.00 24.40 . 1 331 ATOM N ND2 ASN A 47 . 8.947 1.951 7.864 1.00 21.53 . 1 332 ATOM N N HIS A 48 . 12.330 −0.711 10.603 1.00 16.55 . 1 333 ATOM C CA HIS A 48 . 13.554 −1.393 11.036 1.00 17.16 . 1 334 ATOM C C HIS A 48 . 13.715 −2.742 10.344 1.00 18.54 . 1 335 ATOM O O HIS A 48 . 14.854 −3.163 10.113 1.00 19.70 . 1 336 ATOM C CB HIS A 48 . 13.539 −1.562 12.561 1.00 17.58 . 1 337 ATOM C CG HIS A 48 . 14.835 −1.985 13.186 1.00 16.78 . 1 338 ATOM N ND1 HIS A 48 . 16.010 −1.251 13.080 1.00 17.16 . 1 339 ATOM C CD2 HIS A 48 . 15.105 −3.000 14.039 1.00 16.40 . 1 340 ATOM C CE1 HIS A 48 . 16.935 −1.795 13.850 1.00 17.53 . 1 341 ATOM N NE2 HIS A 48 . 16.410 −2.862 14.442 1.00 17.62 . 1 342 ATOM N N GLY A 49 . 12.590 −3.377 9.990 1.00 18.74 . 1 343 ATOM C CA GLY A 49 . 12.582 −4.664 9.304 1.00 20.72 . 1 344 ATOM C C GLY A 49 . 12.798 −5.912 10.123 1.00 20.97 . 1 345 ATOM O O GLY A 49 . 12.806 −7.034 9.578 1.00 21.62 . 1 346 ATOM N N LYS A 50 . 12.985 −5.727 11.415 1.00 20.54 . 1 347 ATOM C CA LYS A 50 . 13.208 −6.810 12.356 1.00 19.31 . 1 348 ATOM C C LYS A 50 . 12.854 −6.301 13.758 1.00 19.51 . 1 349 ATOM O O LYS A 50 . 12.649 −5.097 13.954 1.00 17.63 . 1 350 ATOM C CB LYS A 50 . 14.682 −7.234 12.310 1.00 22.81 . 1 351 ATOM C CG LYS A 50 . 15.644 −6.247 12.872 1.00 25.21 . 1 352 ATOM C CD LYS A 50 . 17.027 −6.930 12.855 1.00 29.56 . 1 353 ATOM C CE LYS A 50 . 18.072 −6.066 13.455 1.00 32.22 . 1 354 ATOM N NZ LYS A 50 . 18.763 −5.337 12.356 1.00 35.96 . 1 355 ATOM N N PRO A 51 . 12.798 −7.186 14.764 1.00 19.25 . 1 356 ATOM C CA PRO A 51 . 12.475 −6.712 16.122 1.00 18.88 . 1 357 ATOM C C PRO A 51 . 13.549 −5.699 16.547 1.00 19.81 . 1 358 ATOM O O PRO A 51 . 14.751 −5.874 16.254 1.00 19.07 . 1 359 ATOM C CB PRO A 51 . 12.512 −7.998 16.972 1.00 19.78 . 1 360 ATOM C CG PRO A 51 . 12.077 −9.069 16.002 1.00 20.63 . 1 361 ATOM C CD PRO A 51 . 12.803 −8.658 14.705 1.00 18.75 . 1 362 ATOM N N ILE A 52 . 13.137 −4.626 17.210 1.00 17.99 . 1 363 ATOM C CA ILE A 52 . 14.083 −3.609 17.575 1.00 17.15 . 1 364 ATOM C C ILE A 52 . 14.583 −3.701 19.015 1.00 18.10 . 1 365 ATOM O O ILE A 52 . 13.772 −3.896 19.941 1.00 18.92 . 1 366 ATOM C CB ILE A 52 . 13.481 −2.202 17.293 1.00 16.97 . 1 367 ATOM C CG1 ILE A 52 . 14.558 −1.124 17.399 1.00 16.70 . 1 368 ATOM C CG2 ILE A 52 . 12.416 −1.844 18.322 1.00 16.96 . 1 369 ATOM C CD1 ILE A 52 . 14.150 0.167 16.707 1.00 18.01 . 1 370 ATOM N N SER A 53 . 15.891 −3.544 19.238 1.00 18.07 . 1 371 ATOM C CA SER A 53 . 16.416 −3.611 20.597 1.00 18.31 . 1 372 ATOM C C SER A 53 . 16.002 −2.357 21.376 1.00 18.60 . 1 373 ATOM O O SER A 53 . 15.747 −1.291 20.781 1.00 17.66 . 1 374 ATOM C CB SER A 53 . 17.969 −3.689 20.581 1.00 16.31 . 1 375 ATOM O OG SER A 53 . 18.527 −2.487 20.050 1.00 19.77 . 1 376 ATOM N N LEU A 54 . 15.925 −2.458 22.708 1.00 17.27 . 1 377 ATOM C CA LEU A 54 . 15.574 −1.281 23.484 1.00 18.43 . 1 378 ATOM C C LEU A 54 . 16.589 −0.185 23.197 1.00 18.79 . 1 379 ATOM O O LEU A 54 . 16.222 0.957 23.060 1.00 17.90 . 1 380 ATOM C CB LEU A 54 . 15.584 −1.601 24.995 1.00 19.14 . 1 381 ATOM C CG LEU A 54 . 15.415 −0.416 25.941 1.00 18.37 . 1 382 ATOM C CD1 LEU A 54 . 13.913 0.011 25.821 1.00 19.61 . 1 383 ATOM C CD2 LEU A 54 . 15.735 −0.798 27.420 1.00 20.48 . 1 384 ATOM N N SER A 55 . 17.884 −0.505 23.072 1.00 19.21 . 1 385 ATOM C CA SER A 55 . 18.858 0.568 22.867 1.00 20.31 . 1 386 ATOM C C SER A 55 . 18.685 1.265 21.517 1.00 18.99 . 1 387 ATOM O O SER A 55 . 18.791 2.487 21.440 1.00 20.05 . 1 388 ATOM C CB SER A 55 . 20.284 0.005 23.016 1.00 21.67 . 1 389 ATOM O OG SER A 55 . 20.557 −0.898 21.976 1.00 25.42 . 1 390 ATOM N N ASN A 56 . 18.386 0.503 20.471 1.00 18.71 . 1 391 ATOM C CA ASN A 56 . 18.146 1.109 19.155 1.00 18.84 . 1 392 ATOM C C ASN A 56 . 16.848 1.931 19.188 1.00 18.50 . 1 393 ATOM O O ASN A 56 . 16.772 2.992 18.576 1.00 19.86 . 1 394 ATOM C CB ASN A 56 . 18.057 0.051 18.063 1.00 19.07 . 1 395 ATOM C CG ASN A 56 . 19.436 −0.364 17.551 1.00 20.37 . 1 396 ATOM O OD1 ASN A 56 . 19.600 −1.452 17.007 1.00 21.34 . 1 397 ATOM N ND2 ASN A 56 . 20.404 0.510 17.727 1.00 19.72 . 1 398 ATOM N N LEU A 57 . 15.828 1.422 19.888 1.00 17.14 . 1 399 ATOM C CA LEU A 57 . 14.580 2.159 19.985 1.00 16.78 . 1 400 ATOM C C LEU A 57 . 14.769 3.496 20.664 1.00 17.15 . 1 401 ATOM O O LEU A 57 . 14.314 4.532 20.122 1.00 17.27 . 1 402 ATOM C CB LEU A 57 . 13.521 1.338 20.764 1.00 17.10 . 1 403 ATOM C CG LEU A 57 . 12.174 2.062 20.938 1.00 16.68 . 1 404 ATOM C CD1 LEU A 57 . 11.569 2.378 19.550 1.00 17.67 . 1 405 ATOM C CD2 LEU A 57 . 11.196 1.149 21.759 1.00 18.15 . 1 406 ATOM N N VAL A 58 . 15.394 3.526 21.844 1.00 18.81 . 1 407 ATOM C CA VAL A 58 . 15.534 4.814 22.498 1.00 19.41 . 1 408 ATOM C C VAL A 58 . 16.532 5.697 21.752 1.00 20.39 . 1 409 ATOM O O VAL A 58 . 16.464 6.916 21.886 1.00 20.51 . 1 410 ATOM C CB VAL A 58 . 15.863 4.720 24.021 1.00 21.25 . 1 411 ATOM C CG1 VAL A 58 . 14.793 3.843 24.708 1.00 21.93 . 1 412 ATOM C CG2 VAL A 58 . 17.263 4.184 24.257 1.00 22.20 . 1 413 ATOM N N SER A 59 . 17.410 5.111 20.931 1.00 20.53 . 1 414 ATOM C CA SER A 59 . 18.346 5.927 20.138 1.00 21.39 . 1 415 ATOM C C SER A 59 . 17.515 6.661 19.076 1.00 20.43 . 1 416 ATOM O O SER A 59 . 17.626 7.892 18.898 1.00 20.74 . 1 417 ATOM C CB SER A 59 . 19.376 5.043 19.438 1.00 23.32 . 1 418 ATOM O OG SER A 59 . 20.363 5.869 18.859 1.00 27.03 . 1 419 ATOM N N ILE A 60 . 16.691 5.913 18.367 1.00 19.17 . 1 420 ATOM C CA ILE A 60 . 15.837 6.552 17.364 1.00 17.69 . 1 421 ATOM C C ILE A 60 . 14.896 7.603 17.989 1.00 18.28 . 1 422 ATOM O O ILE A 60 . 14.727 8.694 17.458 1.00 18.77 . 1 423 ATOM C CB ILE A 60 . 14.983 5.526 16.620 1.00 18.63 . 1 424 ATOM C CG1 ILE A 60 . 15.894 4.595 15.821 1.00 18.41 . 1 425 ATOM C CG2 ILE A 60 . 14.008 6.239 15.682 1.00 16.54 . 1 426 ATOM C CD1 ILE A 60 . 15.194 3.564 14.954 1.00 18.29 . 1 427 ATOM N N LEU A 61 . 14.310 7.294 19.144 1.00 16.33 . 1 428 ATOM C CA LEU A 61 . 13.391 8.233 19.781 1.00 17.78 . 1 429 ATOM C C LEU A 61 . 14.063 9.463 20.362 1.00 16.06 . 1 430 ATOM O O LEU A 61 . 13.433 10.514 20.555 1.00 16.11 . 1 431 ATOM C CB LEU A 61 . 12.565 7.534 20.895 1.00 17.08 . 1 432 ATOM C CG LEU A 61 . 11.710 6.327 20.438 1.00 16.83 . 1 433 ATOM C CD1 LEU A 61 . 11.064 5.652 21.643 1.00 15.95 . 1 434 ATOM C CD2 LEU A 61 . 10.605 6.793 19.464 1.00 16.17 . 1 435 ATOM N N GLN A 62 . 15.353 9.339 20.674 1.00 17.47 . 1 436 ATOM C CA GLN A 62 . 16.111 10.428 21.284 1.00 18.38 . 1 437 ATOM C C GLN A 62 . 15.526 10.907 22.633 1.00 17.06 . 1 438 ATOM O O GLN A 62 . 15.447 12.100 22.931 1.00 18.96 . 1 439 ATOM C CB GLN A 62 . 16.278 11.601 20.299 1.00 20.53 . 1 440 ATOM C CG GLN A 62 . 17.238 11.219 19.119 1.00 24.86 . 1 441 ATOM C CD GLN A 62 . 18.708 10.965 19.577 1.00 27.13 . 1 442 ATOM O OE1 GLN A 62 . 19.418 11.907 19.946 1.00 32.23 . 1 443 ATOM N NE2 GLN A 62 . 19.161 9.691 19.555 1.00 29.80 . 1 444 ATOM N N VAL A 63 . 15.062 9.952 23.432 1.00 18.10 . 1 445 ATOM C CA VAL A 63 . 14.561 10.277 24.756 1.00 19.85 . 1 446 ATOM C C VAL A 63 . 15.788 10.450 25.661 1.00 19.84 . 1 447 ATOM O O VAL A 63 . 16.858 9.869 25.389 1.00 19.51 . 1 448 ATOM C CB VAL A 63 . 13.688 9.121 25.372 1.00 20.37 . 1 449 ATOM C CG1 VAL A 63 . 12.429 8.890 24.495 1.00 20.23 . 1 450 ATOM C CG2 VAL A 63 . 14.484 7.837 25.453 1.00 21.74 . 1 451 ATOM N N PRO A 64 . 15.639 11.239 26.731 1.00 18.86 . 1 452 ATOM C CA PRO A 64 . 16.747 11.466 27.666 1.00 20.25 . 1 453 ATOM C C PRO A 64 . 17.054 10.178 28.389 1.00 20.83 . 1 454 ATOM O O PRO A 64 . 16.177 9.350 28.577 1.00 20.45 . 1 455 ATOM C CB PRO A 64 . 16.225 12.560 28.585 1.00 21.29 . 1 456 ATOM C CG PRO A 64 . 14.746 12.507 28.430 1.00 22.05 . 1 457 ATOM C CD PRO A 64 . 14.525 12.175 26.993 1.00 19.99 . 1 458 ATOM N N SER A 65 . 18.313 9.978 28.782 1.00 21.02 . 1 459 ATOM C CA SER A 65 . 18.676 8.723 29.438 1.00 22.09 . 1 460 ATOM C C SER A 65 . 17.863 8.450 30.721 1.00 19.95 . 1 461 ATOM O O SER A 65 . 17.594 7.290 31.028 1.00 20.39 . 1 462 ATOM C CB SER A 65 . 20.177 8.720 29.761 1.00 24.46 . 1 463 ATOM O OG SER A 65 . 20.460 9.796 30.628 1.00 29.77 . 1 464 ATOM N N SER A 66 . 17.475 9.514 31.426 1.00 18.06 . 1 465 ATOM C CA SER A 66 . 16.683 9.409 32.655 1.00 19.13 . 1 466 ATOM C C SER A 66 . 15.295 8.819 32.413 1.00 16.22 . 1 467 ATOM O O SER A 66 . 14.621 8.429 33.374 1.00 17.14 . 1 468 ATOM C CB SER A 66 . 16.524 10.769 33.293 1.00 18.70 . 1 469 ATOM O OG SER A 66 . 15.745 11.658 32.487 1.00 21.65 . 1 470 ATOM N N LYS A 67 . 14.853 8.796 31.153 1.00 17.27 . 1 471 ATOM C CA LYS A 67 . 13.542 8.232 30.827 1.00 16.28 . 1 472 ATOM C C LYS A 67 . 13.600 6.948 30.008 1.00 16.06 . 1 473 ATOM O O LYS A 67 . 12.575 6.372 29.617 1.00 15.40 . 1 474 ATOM C CB LYS A 67 . 12.666 9.263 30.104 1.00 15.09 . 1 475 ATOM C CG LYS A 67 . 12.288 10.442 30.951 1.00 16.17 . 1 476 ATOM C CD LYS A 67 . 11.297 10.060 32.080 1.00 15.58 . 1 477 ATOM C CE LYS A 67 . 11.023 11.146 33.086 1.00 16.47 . 1 478 ATOM N NZ LYS A 67 . 10.495 12.399 32.620 1.00 16.54 . 1 479 ATOM N N ILE A 68 . 14.790 6.440 29.737 1.00 15.65 . 1 480 ATOM C CA ILE A 68 . 14.903 5.189 29.010 1.00 16.46 . 1 481 ATOM C C ILE A 68 . 14.179 4.040 29.756 1.00 15.56 . 1 482 ATOM O O ILE A 68 . 13.495 3.220 29.140 1.00 15.64 . 1 483 ATOM C CB ILE A 68 . 16.415 4.830 28.739 1.00 16.24 . 1 484 ATOM C CG1 ILE A 68 . 16.956 5.814 27.691 1.00 18.00 . 1 485 ATOM C CG2 ILE A 68 . 16.564 3.363 28.314 1.00 17.93 . 1 486 ATOM C CD1 ILE A 68 . 18.477 5.713 27.556 1.00 19.06 . 1 487 ATOM N N GLY A 69 . 14.394 3.938 31.081 1.00 16.92 . 1 488 ATOM C CA GLY A 69 . 13.732 2.885 31.858 1.00 15.44 . 1 489 ATOM C C GLY A 69 . 12.216 3.003 31.772 1.00 14.09 . 1 490 ATOM O O GLY A 69 . 11.532 1.997 31.743 1.00 15.18 . 1 491 ATOM N N ASN A 70 . 11.737 4.234 31.695 1.00 15.33 . 1 492 ATOM C CA ASN A 70 . 10.298 4.437 31.544 1.00 14.18 . 1 493 ATOM C C ASN A 70 . 9.805 3.960 30.167 1.00 13.67 . 1 494 ATOM O O ASN A 70 . 8.711 3.411 30.061 1.00 13.75 . 1 495 ATOM C CB ASN A 70 . 9.995 5.889 31.801 1.00 12.89 . 1 496 ATOM C CG ASN A 70 . 10.101 6.230 33.270 1.00 16.35 . 1 497 ATOM O OD1 ASN A 70 . 9.276 5.750 34.102 1.00 20.23 . 1 498 ATOM N ND2 ASN A 70 . 11.091 7.044 33.621 1.00 14.41 . 1 499 ATOM N N VAL A 71 . 10.625 4.127 29.117 1.00 14.22 . 1 500 ATOM C CA VAL A 71 . 10.235 3.616 27.823 1.00 14.48 . 1 501 ATOM C C VAL A 71 . 10.136 2.078 27.957 1.00 14.62 . 1 502 ATOM O O VAL A 71 . 9.216 1.439 27.445 1.00 14.60 . 1 503 ATOM C CB VAL A 71 . 11.301 4.013 26.733 1.00 13.91 . 1 504 ATOM C CG1 VAL A 71 . 11.000 3.261 25.461 1.00 14.06 . 1 505 ATOM C CG2 VAL A 71 . 11.199 5.515 26.441 1.00 15.01 . 1 506 ATOM N N ARG A 72 . 11.141 1.442 28.582 1.00 14.14 . 1 507 ATOM C CA ARG A 72 . 11.118 −0.015 28.741 1.00 14.40 . 1 508 ATOM C C ARG A 72 . 9.873 −0.473 29.537 1.00 12.39 . 1 509 ATOM O O ARG A 72 . 9.245 −1.485 29.177 1.00 14.30 . 1 510 ATOM C CB ARG A 72 . 12.389 −0.465 29.505 1.00 16.97 . 1 511 ATOM C CG ARG A 72 . 12.518 −1.985 29.685 1.00 19.78 . 1 512 ATOM C CD ARG A 72 . 13.690 −2.424 30.685 1.00 23.10 . 1 513 ATOM N NE ARG A 72 . 13.977 −1.469 31.790 1.00 28.99 . 1 514 ATOM C CZ ARG A 72 . 13.267 −1.280 32.910 1.00 30.05 . 1 515 ATOM N NH1 ARG A 72 . 12.164 −1.987 33.166 1.00 33.28 . 1 516 ATOM N NH2 ARG A 72 . 13.644 −0.336 33.769 1.00 31.90 . 1 517 ATOM N N ARG A 73 . 9.548 0.262 30.593 1.00 15.28 . 1 518 ATOM C CA ARG A 73 . 8.386 −0.163 31.402 1.00 14.87 . 1 519 ATOM C C ARG A 73 . 7.081 −0.081 30.588 1.00 15.00 . 1 520 ATOM O O ARG A 73 . 6.226 −0.974 30.653 1.00 16.14 . 1 521 ATOM C CB ARG A 73 . 8.326 0.670 32.687 1.00 15.78 . 1 522 ATOM C CG ARG A 73 . 9.397 0.216 33.707 1.00 16.43 . 1 523 ATOM C CD ARG A 73 . 9.872 1.296 34.628 1.00 16.64 . 1 524 ATOM N NE ARG A 73 . 8.857 1.894 35.521 1.00 20.15 . 1 525 ATOM C CZ ARG A 73 . 9.041 2.982 36.301 1.00 20.51 . 1 526 ATOM N NH1 ARG A 73 . 10.203 3.661 36.346 1.00 22.95 . 1 527 ATOM N NH2 ARG A 73 . 8.029 3.384 37.061 1.00 19.36 . 1 528 ATOM N N LEU A 74 . 6.951 0.976 29.804 1.00 13.79 . 1 529 ATOM C CA LEU A 74 . 5.762 1.126 28.946 1.00 13.78 . 1 530 ATOM C C LEU A 74 . 5.723 0.073 27.848 1.00 14.17 . 1 531 ATOM O O LEU A 74 . 4.651 −0.456 27.521 1.00 15.17 . 1 532 ATOM C CB LEU A 74 . 5.718 2.560 28.367 1.00 12.41 . 1 533 ATOM C CG LEU A 74 . 5.220 3.630 29.337 1.00 12.58 . 1 534 ATOM C CD1 LEU A 74 . 5.589 5.056 28.946 1.00 12.29 . 1 535 ATOM C CD2 LEU A 74 . 3.692 3.534 29.336 1.00 13.51 . 1 536 ATOM N N MET A 75 . 6.877 −0.233 27.232 1.00 13.18 . 1 537 ATOM C CA MET A 75 . 6.895 −1.242 26.195 1.00 14.13 . 1 538 ATOM C C MET A 75 . 6.487 −2.620 26.696 1.00 13.78 . 1 539 ATOM O O MET A 75 . 5.818 −3.372 25.992 1.00 14.81 . 1 540 ATOM C CB MET A 75 . 8.265 −1.319 25.492 1.00 14.48 . 1 541 ATOM C CG MET A 75 . 8.530 −0.091 24.610 1.00 14.91 . 1 542 ATOM S SD MET A 75 . 7.386 0.131 23.184 1.00 14.94 . 1 543 ATOM C CE MET A 75 . 7.812 −1.285 22.204 1.00 13.93 . 1 544 ATOM N N ARG A 76 . 6.978 −2.965 27.883 1.00 15.94 . 1 545 ATOM C CA ARG A 76 . 6.644 −4.268 28.450 1.00 17.39 . 1 546 ATOM C C ARG A 76 . 5.160 −4.346 28.807 1.00 16.16 . 1 547 ATOM O O ARG A 76 . 4.541 −5.405 28.587 1.00 17.14 . 1 548 ATOM C CB ARG A 76 . 7.501 −4.480 29.671 1.00 15.76 . 1 549 ATOM C CG ARG A 76 . 8.946 −4.679 29.305 1.00 19.30 . 1 550 ATOM C CD ARG A 76 . 9.772 −4.852 30.565 1.00 20.35 . 1 551 ATOM N NE ARG A 76 . 11.105 −5.372 30.254 1.00 20.70 . 1 552 ATOM C CZ ARG A 76 . 11.970 −5.811 31.185 1.00 23.51 . 1 553 ATOM N NH1 ARG A 76 . 11.651 −5.791 32.476 1.00 24.59 . 1 554 ATOM N NH2 ARG A 76 . 13.146 −6.304 30.817 1.00 24.58 . 1 555 ATOM N N TYR A 77 . 4.601 −3.222 29.248 1.00 16.04 . 1 556 ATOM C CA TYR A 77 . 3.160 −3.158 29.594 1.00 13.94 . 1 557 ATOM C C TYR A 77 . 2.346 −3.331 28.295 1.00 15.92 . 1 558 ATOM O O TYR A 77 . 1.389 −4.144 28.242 1.00 15.32 . 1 559 ATOM C CB TYR A 77 . 2.864 −1.830 30.258 1.00 15.28 . 1 560 ATOM C CG TYR A 77 . 1.433 −1.692 30.721 1.00 14.99 . 1 561 ATOM C CD1 TYR A 77 . 1.032 −2.157 31.950 1.00 15.69 . 1 562 ATOM C CD2 TYR A 77 . 0.466 −1.112 29.880 1.00 16.56 . 1 563 ATOM C CE1 TYR A 77 . −0.303 −2.068 32.370 1.00 17.59 . 1 564 ATOM C CE2 TYR A 77 . −0.881 −1.016 30.286 1.00 17.99 . 1 565 ATOM C CZ TYR A 77 . −1.250 −1.499 31.530 1.00 17.00 . 1 566 ATOM O OH TYR A 77 . −2.554 −1.410 31.964 1.00 21.24 . 1 567 ATOM N N LEU A 78 . 2.724 −2.613 27.228 1.00 14.17 . 1 568 ATOM C CA LEU A 78 . 2.036 −2.785 25.950 1.00 15.48 . 1 569 ATOM C C LEU A 78 . 2.223 −4.198 25.371 1.00 15.51 . 1 570 ATOM O O LEU A 78 . 1.326 −4.760 24.705 1.00 15.79 . 1 571 ATOM C CB LEU A 78 . 2.550 −1.754 24.962 1.00 15.86 . 1 572 ATOM C CG LEU A 78 . 2.001 −0.361 25.259 1.00 14.27 . 1 573 ATOM C CD1 LEU A 78 . 2.942 0.654 24.717 1.00 15.62 . 1 574 ATOM C CD2 LEU A 78 . 0.610 −0.202 24.633 1.00 17.23 . 1 575 ATOM N N ALA A 79 . 3.406 −4.786 25.583 1.00 15.16 . 1 576 ATOM C CA ALA A 79 . 3.632 −6.135 25.050 1.00 17.19 . 1 577 ATOM C C ALA A 79 . 2.716 −7.178 25.725 1.00 17.39 . 1 578 ATOM O O ALA A 79 . 2.099 −8.006 25.051 1.00 17.42 . 1 579 ATOM C CB ALA A 79 . 5.128 −6.553 25.228 1.00 16.03 . 1 580 ATOM N N HIS A 80 . 2.611 −7.108 27.035 1.00 18.93 . 1 581 ATOM C CA HIS A 80 . 1.755 −8.029 27.775 1.00 19.30 . 1 582 ATOM C C HIS A 80 . 0.305 −7.880 27.290 1.00 19.80 . 1 583 ATOM O O HIS A 80 . −0.444 −8.849 27.229 1.00 20.57 . 1 584 ATOM C CB HIS A 80 . 1.866 −7.751 29.264 1.00 19.30 . 1 585 ATOM C CG HIS A 80 . 1.012 −8.673 30.070 1.00 22.67 . 1 586 ATOM N ND1 HIS A 80 . −0.247 −8.328 30.502 1.00 24.66 . 1 587 ATOM C CD2 HIS A 80 . 1.188 −9.976 30.404 1.00 24.83 . 1 588 ATOM C CE1 HIS A 80 . −0.818 −9.381 31.070 1.00 25.60 . 1 589 ATOM N NE2 HIS A 80 . 0.028 −10.393 31.019 1.00 24.85 . 1 590 ATOM N N ASN A 81 . −0.073 −6.671 26.901 1.00 20.01 . 1 591 ATOM C CA ASN A 81 . −1.409 −6.456 26.348 1.00 18.60 . 1 592 ATOM C C ASN A 81 . −1.583 −6.971 24.955 1.00 18.77 . 1 593 ATOM O O ASN A 81 . −2.706 −7.028 24.469 1.00 20.58 . 1 594 ATOM C CB ASN A 81 . −1.793 −4.986 26.396 1.00 18.25 . 1 595 ATOM C CG ASN A 81 . −2.262 −4.580 27.751 1.00 20.12 . 1 596 ATOM O OD1 ASN A 81 . −2.759 −5.417 28.509 1.00 22.20 . 1 597 ATOM N ND2 ASN A 81 . −2.143 −3.301 28.072 1.00 19.50 . 1 598 ATOM N N GLY A 82 . −0.495 −7.343 24.288 1.00 17.03 . 1 599 ATOM C CA GLY A 82 . −0.622 −7.918 22.969 1.00 17.16 . 1 600 ATOM C C GLY A 82 . −0.206 −7.062 21.824 1.00 14.66 . 1 601 ATOM O O GLY A 82 . −0.410 −7.445 20.673 1.00 17.94 . 1 602 ATOM N N PHE A 83 . 0.341 −5.899 22.127 1.00 17.05 . 1 603 ATOM C CA PHE A 83 . 0.724 −5.014 21.047 1.00 15.80 . 1 604 ATOM C C PHE A 83 . 2.139 −5.158 20.561 1.00 16.07 . 1 605 ATOM O O PHE A 83 . 2.475 −4.600 19.547 1.00 16.37 . 1 606 ATOM C CB PHE A 83 . 0.426 −3.538 21.429 1.00 16.22 . 1 607 ATOM C CG PHE A 83 . −1.027 −3.264 21.616 1.00 17.05 . 1 608 ATOM C CD1 PHE A 83 . −1.601 −3.184 22.891 1.00 16.78 . 1 609 ATOM C CD2 PHE A 83 . −1.854 −3.192 20.491 1.00 19.05 . 1 610 ATOM C CE1 PHE A 83 . −2.997 −3.044 23.059 1.00 18.87 . 1 611 ATOM C CE2 PHE A 83 . −3.233 −3.047 20.628 1.00 19.85 . 1 612 ATOM C CZ PHE A 83 . −3.819 −2.972 21.906 1.00 18.40 . 1 613 ATOM N N PHE A 84 . 2.977 −5.904 21.280 1.00 16.04 . 1 614 ATOM C CA PHE A 84 . 4.341 −6.142 20.839 1.00 16.51 . 1 615 ATOM C C PHE A 84 . 4.697 −7.535 21.368 1.00 17.05 . 1 616 ATOM O O PHE A 84 . 4.075 −8.024 22.332 1.00 17.99 . 1 617 ATOM C CB PHE A 84 . 5.328 −5.134 21.459 1.00 16.34 . 1 618 ATOM C CG PHE A 84 . 5.108 −3.720 21.011 1.00 16.22 . 1 619 ATOM C CD1 PHE A 84 . 4.582 −2.807 21.887 1.00 16.00 . 1 620 ATOM C CD2 PHE A 84 . 5.359 −3.328 19.683 1.00 15.91 . 1 621 ATOM C CE1 PHE A 84 . 4.285 −1.485 21.458 1.00 16.82 . 1 622 ATOM C CE2 PHE A 84 . 5.069 −2.035 19.251 1.00 15.07 . 1 623 ATOM C CZ PHE A 84 . 4.532 −1.114 20.127 1.00 18.23 . 1 624 ATOM N N GLU A 85 . 5.658 −8.168 20.704 1.00 19.01 . 1 625 ATOM C CA GLU A 85 . 6.155 −9.451 21.178 1.00 19.65 . 1 626 ATOM C C GLU A 85 . 7.596 −9.210 21.644 1.00 20.53 . 1 627 ATOM O O GLU A 85 . 8.410 −8.697 20.868 1.00 19.87 . 1 628 ATOM C CB GLU A 85 . 6.158 −10.479 20.066 1.00 22.22 . 1 629 ATOM C CG GLU A 85 . 6.694 −11.812 20.551 1.00 25.54 . 1 630 ATOM C CD GLU A 85 . 7.086 −12.701 19.414 1.00 29.97 . 1 631 ATOM O OE1 GLU A 85 . 6.659 −12.443 18.271 1.00 31.09 . 1 632 ATOM O OE2 GLU A 85 . 7.842 −13.673 19.670 1.00 33.05 . 1 633 ATOM N N ILE A 86 . 7.927 −9.582 22.886 1.00 20.13 . 1 634 ATOM C CA ILE A 86 . 9.292 −9.411 23.378 1.00 21.76 . 1 635 ATOM C C ILE A 86 . 10.106 −10.646 22.972 1.00 23.97 . 1 636 ATOM O O ILE A 86 . 9.647 −11.781 23.124 1.00 23.74 . 1 637 ATOM C CB ILE A 86 . 9.335 −9.230 24.949 1.00 22.04 . 1 638 ATOM C CG1 ILE A 86 . 8.668 −7.912 25.343 1.00 22.88 . 1 639 ATOM C CG2 ILE A 86 . 10.794 −9.166 25.480 1.00 23.73 . 1 640 ATOM C CD1 ILE A 86 . 8.574 −7.686 26.830 1.00 22.44 . 1 641 ATOM N N ILE A 87 . 11.277 −10.391 22.396 1.00 24.88 . 1 642 ATOM C CA ILE A 87 . 12.198 −11.445 21.988 1.00 29.02 . 1 643 ATOM C C ILE A 87 . 13.459 −11.133 22.772 1.00 30.27 . 1 644 ATOM O O ILE A 87 . 13.949 −10.012 22.744 1.00 31.11 . 1 645 ATOM C CB ILE A 87 . 12.422 −11.395 20.471 1.00 30.12 . 1 646 ATOM C CG1 ILE A 87 . 11.086 −11.752 19.802 1.00 31.39 . 1 647 ATOM C CG2 ILE A 87 . 13.531 −12.380 20.034 1.00 31.55 . 1 648 ATOM C CD1 ILE A 87 . 11.093 −11.819 18.294 1.00 34.13 . 1 649 ATOM N N THR A 88 . 13.978 −12.120 23.496 1.00 32.35 . 1 650 ATOM C CA THR A 88 . 15.185 −11.901 24.296 1.00 34.39 . 1 651 ATOM C C THR A 88 . 16.370 −12.735 23.809 1.00 35.75 . 1 652 ATOM O O THR A 88 . 16.227 −13.931 23.567 1.00 35.73 . 1 653 ATOM C CB THR A 88 . 14.927 −12.258 25.742 1.00 35.24 . 1 654 ATOM O OG1 THR A 88 . 13.795 −11.522 26.191 1.00 35.50 . 1 655 ATOM C CG2 THR A 88 . 16.136 −11.910 26.618 1.00 35.32 . 1 656 ATOM N N LYS A 89 . 17.513 −12.074 23.644 1.00 36.85 . 1 657 ATOM C CA LYS A 89 . 18.769 −12.698 23.210 1.00 38.59 . 1 658 ATOM C C LYS A 89 . 19.801 −11.878 23.973 1.00 38.91 . 1 659 ATOM O O LYS A 89 . 19.683 −11.679 25.176 1.00 40.02 . 1 660 ATOM C CB LYS A 89 . 19.034 −12.493 21.713 1.00 38.91 . 1 661 ATOM C CG LYS A 89 . 17.830 −12.513 20.790 1.00 41.01 . 1 662 ATOM C CD LYS A 89 . 17.522 −13.876 20.222 1.00 41.33 . 1 663 ATOM C CE LYS A 89 . 17.106 −13.785 18.755 1.00 41.24 . 1 664 ATOM N NZ LYS A 89 . 16.401 −15.040 18.308 1.00 42.82 . 1 665 ATOM N N GLU A 90 . 20.795 −11.358 23.270 1.00 39.47 . 1 666 ATOM C CA GLU A 90 . 21.768 −10.543 23.963 1.00 39.98 . 1 667 ATOM C C GLU A 90 . 21.061 −9.327 24.567 1.00 38.66 . 1 668 ATOM O O GLU A 90 . 21.486 −8.790 25.591 1.00 39.34 . 1 669 ATOM C CB GLU A 90 . 22.895 −10.107 23.010 1.00 41.72 . 1 670 ATOM C CG GLU A 90 . 24.070 −11.094 22.953 1.00 44.28 . 1 671 ATOM C CD GLU A 90 . 24.673 −11.363 24.333 1.00 45.67 . 1 672 ATOM O OE1 GLU A 90 . 25.755 −11.999 24.425 1.00 47.04 . 1 673 ATOM O OE2 GLU A 90 . 24.057 −10.939 25.344 1.00 48.14 . 1 674 ATOM N N GLU A 91 . 19.972 −8.905 23.931 1.00 37.28 . 1 675 ATOM C CA GLU A 91 . 19.226 −7.759 24.426 1.00 34.57 . 1 676 ATOM C C GLU A 91 . 17.742 −8.089 24.358 1.00 31.72 . 1 677 ATOM O O GLU A 91 . 17.343 −9.095 23.799 1.00 32.32 . 1 678 ATOM C CB GLU A 91 . 19.452 −6.500 23.550 1.00 36.03 . 1 679 ATOM C CG GLU A 91 . 20.843 −5.841 23.596 1.00 38.03 . 1 680 ATOM C CD GLU A 91 . 20.989 −4.703 22.583 1.00 38.35 . 1 681 ATOM O OE1 GLU A 91 . 20.791 −3.520 22.938 1.00 38.67 . 1 682 ATOM O OE2 GLU A 91 . 21.299 −5.000 21.407 1.00 40.68 . 1 683 ATOM N N GLU A 92 . 16.936 −7.227 24.963 1.00 29.21 . 1 684 ATOM C CA GLU A 92 . 15.489 −7.373 24.862 1.00 25.52 . 1 685 ATOM C C GLU A 92 . 15.107 −6.604 23.582 1.00 23.69 . 1 686 ATOM O O GLU A 92 . 15.529 −5.451 23.410 1.00 24.59 . 1 687 ATOM C CB GLU A 92 . 14.833 −6.716 26.066 1.00 26.25 . 1 688 ATOM C CG GLU A 92 . 13.309 −6.621 25.964 1.00 24.96 . 1 689 ATOM C CD GLU A 92 . 12.668 −6.462 27.326 1.00 26.53 . 1 690 ATOM O OE1 GLU A 92 . 12.871 −7.342 28.182 1.00 27.79 . 1 691 ATOM O OE2 GLU A 92 . 11.968 −5.456 27.548 1.00 25.63 . 1 692 ATOM N N SER A 93 . 14.332 −7.246 22.712 1.00 20.55 . 1 693 ATOM C CA SER A 93 . 13.879 −6.634 21.466 1.00 19.86 . 1 694 ATOM C C SER A 93 . 12.352 −6.679 21.385 1.00 19.44 . 1 695 ATOM O O SER A 93 . 11.713 −7.512 22.039 1.00 19.73 . 1 696 ATOM C CB SER A 93 . 14.510 −7.336 20.275 1.00 20.70 . 1 697 ATOM O OG SER A 93 . 15.880 −7.044 20.267 1.00 25.21 . 1 698 ATOM N N TYR A 94 . 11.774 −5.780 20.583 1.00 17.72 . 1 699 ATOM C CA TYR A 94 . 10.322 −5.685 20.427 1.00 17.42 . 1 700 ATOM C C TYR A 94 . 9.886 −5.869 19.013 1.00 18.12 . 1 701 ATOM O O TYR A 94 . 10.352 −5.134 18.138 1.00 17.66 . 1 702 ATOM C CB TYR A 94 . 9.864 −4.303 20.903 1.00 17.39 . 1 703 ATOM C CG TYR A 94 . 10.357 −3.962 22.279 1.00 14.99 . 1 704 ATOM C CD1 TYR A 94 . 11.336 −3.015 22.461 1.00 17.95 . 1 705 ATOM C CD2 TYR A 94 . 9.879 −4.652 23.417 1.00 16.49 . 1 706 ATOM C CE1 TYR A 94 . 11.839 −2.728 23.704 1.00 18.05 . 1 707 ATOM C CE2 TYR A 94 . 10.405 −4.384 24.691 1.00 16.86 . 1 708 ATOM C CZ TYR A 94 . 11.375 −3.418 24.825 1.00 17.77 . 1 709 ATOM O OH TYR A 94 . 11.910 −3.092 26.041 1.00 18.88 . 1 710 ATOM N N ALA A 95 . 8.967 −6.818 18.797 1.00 16.47 . 1 711 ATOM C CA ALA A 95 . 8.442 −7.115 17.486 1.00 17.09 . 1 712 ATOM C C ALA A 95 . 6.987 −6.726 17.376 1.00 16.41 . 1 713 ATOM O O ALA A 95 . 6.283 −6.721 18.371 1.00 16.73 . 1 714 ATOM C CB ALA A 95 . 8.581 −8.633 17.168 1.00 18.84 . 1 715 ATOM N N LEU A 96 . 6.539 −6.380 16.176 1.00 16.11 . 1 716 ATOM C CA LEU A 96 . 5.114 −6.094 15.963 1.00 18.10 . 1 717 ATOM C C LEU A 96 . 4.304 −7.380 16.147 1.00 19.22 . 1 718 ATOM O O LEU A 96 . 4.856 −8.483 16.105 1.00 19.34 . 1 719 ATOM C CB LEU A 96 . 4.863 −5.642 14.529 1.00 20.40 . 1 720 ATOM C CG LEU A 96 . 5.539 −4.337 14.166 1.00 22.34 . 1 721 ATOM C CD1 LEU A 96 . 5.414 −4.120 12.626 1.00 24.38 . 1 722 ATOM C CD2 LEU A 96 . 4.919 −3.235 15.056 1.00 23.37 . 1 723 ATOM N N THR A 97 . 3.002 −7.207 16.372 1.00 18.48 . 1 724 ATOM C CA THR A 97 . 2.046 −8.293 16.461 1.00 19.25 . 1 725 ATOM C C THR A 97 . 0.942 −7.948 15.452 1.00 19.51 . 1 726 ATOM O O THR A 97 . 0.964 −6.883 14.823 1.00 19.26 . 1 727 ATOM C CB THR A 97 . 1.380 −8.411 17.849 1.00 19.57 . 1 728 ATOM O OG1 THR A 97 . 0.616 −7.212 18.124 1.00 20.23 . 1 729 ATOM C CG2 THR A 97 . 2.397 −8.693 18.931 1.00 20.52 . 1 730 ATOM N N VAL A 98 . −0.021 −8.838 15.260 1.00 19.51 . 1 731 ATOM C CA VAL A 98 . −1.055 −8.517 14.304 1.00 19.09 . 1 732 ATOM C C VAL A 98 . −1.794 −7.264 14.746 1.00 17.95 . 1 733 ATOM O O VAL A 98 . −2.194 −6.486 13.899 1.00 18.60 . 1 734 ATOM C CB VAL A 98 . −2.035 −9.678 14.108 1.00 18.57 . 1 735 ATOM C CG1 VAL A 98 . −3.082 −9.288 13.121 1.00 18.56 . 1 736 ATOM C CG2 VAL A 98 . −1.239 −10.929 13.638 1.00 22.14 . 1 737 ATOM N N ALA A 99 . −1.967 −7.078 16.050 1.00 18.31 . 1 738 ATOM C CA ALA A 99 . −2.652 −5.904 16.562 1.00 17.83 . 1 739 ATOM C C ALA A 99 . −1.859 −4.591 16.318 1.00 17.50 . 1 740 ATOM O O ALA A 99 . −2.452 −3.545 15.920 1.00 18.30 . 1 741 ATOM C CB ALA A 99 . −2.973 −6.095 18.057 1.00 17.44 . 1 742 ATOM N N SER A 100 . −0.547 −4.598 16.508 1.00 16.35 . 1 743 ATOM C CA SER A 100 . 0.170 −3.352 16.231 1.00 17.64 . 1 744 ATOM C C SER A 100 . 0.423 −3.179 14.714 1.00 18.01 . 1 745 ATOM O O SER A 100 . 0.742 −2.096 14.246 1.00 17.90 . 1 746 ATOM C CB SER A 100 . 1.471 −3.251 17.042 1.00 17.05 . 1 747 ATOM O OG SER A 100 . 2.273 −4.413 16.856 1.00 17.53 . 1 748 ATOM N N GLU A 101 . 0.256 −4.229 13.921 1.00 18.98 . 1 749 ATOM C CA GLU A 101 . 0.378 −4.061 12.472 1.00 19.00 . 1 750 ATOM C C GLU A 101 . −0.812 −3.202 12.005 1.00 17.29 . 1 751 ATOM O O GLU A 101 . −0.747 −2.565 10.954 1.00 18.72 . 1 752 ATOM C CB GLU A 101 . 0.384 −5.416 11.747 1.00 21.42 . 1 753 ATOM C CG GLU A 101 . 1.715 −6.206 11.872 1.00 24.17 . 1 754 ATOM C CD GLU A 101 . 1.642 −7.629 11.247 1.00 28.12 . 1 755 ATOM O OE1 GLU A 101 . 0.606 −8.018 10.688 1.00 30.74 . 1 756 ATOM O OE2 GLU A 101 . 2.641 −8.364 11.330 1.00 34.08 . 1 757 ATOM N N LEU A 102 . −1.904 −3.203 12.770 1.00 16.33 . 1 758 ATOM C CA LEU A 102 . −3.054 −2.365 12.436 1.00 16.96 . 1 759 ATOM C C LEU A 102 . −2.702 −0.898 12.645 1.00 15.89 . 1 760 ATOM O O LEU A 102 . −3.524 −0.037 12.335 1.00 16.51 . 1 761 ATOM C CB LEU A 102 . −4.291 −2.667 13.328 1.00 17.36 . 1 762 ATOM C CG LEU A 102 . −4.976 −4.051 13.209 1.00 19.46 . 1 763 ATOM C CD1 LEU A 102 . −5.930 −4.299 14.373 1.00 21.87 . 1 764 ATOM C CD2 LEU A 102 . −5.697 −4.161 11.877 1.00 20.00 . 1 765 ATOM N N LEU A 103 . −1.530 −0.601 13.208 1.00 14.47 . 1 766 ATOM C CA LEU A 103 . −1.136 0.811 13.499 1.00 14.73 . 1 767 ATOM C C LEU A 103 . −0.032 1.318 12.544 1.00 13.94 . 1 768 ATOM O O LEU A 103 . 0.385 2.447 12.648 1.00 15.21 . 1 769 ATOM C CB LEU A 103 . −0.657 0.939 14.966 1.00 13.49 . 1 770 ATOM C CG LEU A 103 . −1.658 0.431 16.029 1.00 15.43 . 1 771 ATOM C CD1 LEU A 103 . −0.995 0.419 17.417 1.00 16.01 . 1 772 ATOM C CD2 LEU A 103 . −2.923 1.263 16.062 1.00 14.13 . 1 773 ATOM N N VAL A 104 . 0.367 0.462 11.601 1.00 15.65 . 1 774 ATOM C CA VAL A 104 . 1.440 0.774 10.651 1.00 16.74 . 1 775 ATOM C C VAL A 104 . 0.865 1.436 9.422 1.00 18.61 . 1 776 ATOM O O VAL A 104 . −0.068 0.936 8.799 1.00 18.19 . 1 777 ATOM C CB VAL A 104 . 2.165 −0.524 10.299 1.00 16.80 . 1 778 ATOM C CG1 VAL A 104 . 3.185 −0.327 9.134 1.00 16.42 . 1 779 ATOM C CG2 VAL A 104 . 2.866 −1.036 11.507 1.00 17.01 . 1 780 ATOM N N ARG A 105 . 1.421 2.595 9.110 1.00 21.60 . 1 781 ATOM C CA ARG A 105 . 0.972 3.390 7.965 1.00 26.05 . 1 782 ATOM C C ARG A 105 . 1.080 2.632 6.682 1.00 28.83 . 1 783 ATOM O O ARG A 105 . 2.030 1.896 6.479 1.00 29.85 . 1 784 ATOM C CB ARG A 105 . 1.845 4.616 7.771 1.00 28.57 . 1 785 ATOM C CG ARG A 105 . 1.835 5.604 8.881 1.00 34.52 . 1 786 ATOM C CD ARG A 105 . 2.544 6.899 8.468 1.00 38.33 . 1 787 ATOM N NE ARG A 105 . 1.970 7.997 9.239 1.00 42.39 . 1 788 ATOM C CZ ARG A 105 . 2.644 9.080 9.629 1.00 44.22 . 1 789 ATOM N NH1 ARG A 105 . 3.941 9.205 9.318 1.00 44.08 . 1 790 ATOM N NH2 ARG A 105 . 2.020 10.044 10.327 1.00 44.53 . 1 791 ATOM N N GLY A 106 . 0.131 2.831 5.797 1.00 30.94 . 1 792 ATOM C CA GLY A 106 . 0.266 2.162 4.523 1.00 35.55 . 1 793 ATOM C C GLY A 106 . 0.131 0.663 4.611 1.00 37.35 . 1 794 ATOM O O GLY A 106 . 0.357 −0.052 3.631 1.00 38.95 . 1 795 ATOM N N SER A 107 . −0.200 0.169 5.795 1.00 38.54 . 1 796 ATOM C CA SER A 107 . −0.446 −1.246 5.945 1.00 38.46 . 1 797 ATOM C C SER A 107 . −1.835 −1.313 5.264 1.00 37.99 . 1 798 ATOM O O SER A 107 . −2.421 −0.269 4.997 1.00 38.13 . 1 799 ATOM C CB SER A 107 . −0.505 −1.597 7.433 1.00 39.43 . 1 800 ATOM O OG SER A 107 . −1.828 −1.851 7.861 1.00 40.05 . 1 801 ATOM N N ASP A 108 . −2.337 −2.505 4.946 1.00 37.48 . 1 802 ATOM C CA ASP A 108 . −3.649 −2.648 4.286 1.00 36.84 . 1 803 ATOM C C ASP A 108 . −4.795 −1.963 5.039 1.00 35.33 . 1 804 ATOM O O ASP A 108 . −5.588 −1.217 4.454 1.00 36.07 . 1 805 ATOM C CB ASP A 108 . −4.000 −4.136 4.135 1.00 39.68 . 1 806 ATOM C CG ASP A 108 . −3.632 −4.704 2.768 1.00 41.48 . 1 807 ATOM O OD1 ASP A 108 . −2.452 −4.643 2.373 1.00 44.12 . 1 808 ATOM O OD2 ASP A 108 . −4.530 −5.233 2.090 1.00 43.07 . 1 809 ATOM N N LEU A 109 . −4.903 −2.270 6.335 1.00 32.32 . 1 810 ATOM C CA LEU A 109 . −5.921 −1.700 7.201 1.00 27.42 . 1 811 ATOM C C LEU A 109 . −5.185 −1.001 8.344 1.00 26.37 . 1 812 ATOM O O LEU A 109 . −4.610 −1.651 9.217 1.00 26.30 . 1 813 ATOM C CB LEU A 109 . −6.811 −2.795 7.791 1.00 28.65 . 1 814 ATOM C CG LEU A 109 . −7.837 −2.348 8.832 1.00 27.90 . 1 815 ATOM C CD1 LEU A 109 . −8.878 −1.431 8.183 1.00 30.73 . 1 816 ATOM C CD2 LEU A 109 . −8.495 −3.551 9.454 1.00 29.19 . 1 817 ATOM N N CYS A 110 . −5.224 0.323 8.358 1.00 21.60 . 1 818 ATOM C CA CYS A 110 . −4.521 1.087 9.402 1.00 18.96 . 1 819 ATOM C C CYS A 110 . −5.504 1.865 10.258 1.00 18.12 . 1 820 ATOM O O CYS A 110 . −6.132 2.804 9.744 1.00 19.22 . 1 821 ATOM C CB CYS A 110 . −3.546 2.093 8.771 1.00 18.93 . 1 822 ATOM S SG CYS A 110 . −2.597 3.070 9.991 1.00 19.03 . 1 823 ATOM N N LEU A 111 . −5.603 1.512 11.525 1.00 15.61 . 1 824 ATOM C CA LEU A 111 . −6.559 2.160 12.415 1.00 15.33 . 1 825 ATOM C C LEU A 111 . −5.909 3.151 13.362 1.00 15.86 . 1 826 ATOM O O LEU A 111 . −6.552 3.625 14.281 1.00 17.10 . 1 827 ATOM C CB LEU A 111 . −7.334 1.090 13.189 1.00 17.95 . 1 828 ATOM C CG LEU A 111 . −8.013 0.147 12.195 1.00 18.38 . 1 829 ATOM C CD1 LEU A 111 . −8.661 −1.004 12.928 1.00 20.63 . 1 830 ATOM C CD2 LEU A 111 . −9.096 0.977 11.367 1.00 21.61 . 1 831 ATOM N N ALA A 112 . −4.655 3.525 13.112 1.00 15.82 . 1 832 ATOM C CA ALA A 112 . −4.036 4.499 14.039 1.00 16.56 . 1 833 ATOM C C ALA A 112 . −4.845 5.784 14.083 1.00 15.39 . 1 834 ATOM O O ALA A 112 . −4.966 6.385 15.142 1.00 15.98 . 1 835 ATOM C CB ALA A 112 . −2.545 4.820 13.665 1.00 15.56 . 1 836 ATOM N N PRO A 113 . −5.435 6.244 12.955 1.00 15.12 . 1 837 ATOM C CA PRO A 113 . −6.205 7.491 13.085 1.00 14.99 . 1 838 ATOM C C PRO A 113 . −7.403 7.410 14.008 1.00 16.34 . 1 839 ATOM O O PRO A 113 . −7.839 8.422 14.567 1.00 15.54 . 1 840 ATOM C CB PRO A 113 . −6.608 7.824 11.629 1.00 16.75 . 1 841 ATOM C CG PRO A 113 . −5.500 7.226 10.836 1.00 15.78 . 1 842 ATOM C CD PRO A 113 . −5.224 5.887 11.544 1.00 16.98 . 1 843 ATOM N N MET A 114 . −7.930 6.217 14.195 1.00 15.47 . 1 844 ATOM C CA MET A 114 . −9.048 5.993 15.111 1.00 16.48 . 1 845 ATOM C C MET A 114 . −8.539 6.145 16.555 1.00 15.06 . 1 846 ATOM O O MET A 114 . −9.204 6.749 17.402 1.00 15.22 . 1 847 ATOM C CB MET A 114 . −9.619 4.588 14.864 1.00 20.44 . 1 848 ATOM C CG MET A 114 . −10.972 4.267 15.380 1.00 26.18 . 1 849 ATOM S SD MET A 114 . −11.412 2.658 14.528 1.00 32.60 . 1 850 ATOM C CE MET A 114 . −12.291 3.074 12.904 1.00 28.75 . 1 851 ATOM N N VAL A 115 . −7.350 5.614 16.857 1.00 13.60 . 1 852 ATOM C CA VAL A 115 . −6.794 5.759 18.201 1.00 14.03 . 1 853 ATOM C C VAL A 115 . −6.638 7.236 18.523 1.00 13.96 . 1 854 ATOM O O VAL A 115 . −7.049 7.687 19.603 1.00 16.35 . 1 855 ATOM C CB VAL A 115 . −5.391 5.075 18.271 1.00 13.96 . 1 856 ATOM C CG1 VAL A 115 . −4.755 5.283 19.628 1.00 14.83 . 1 857 ATOM C CG2 VAL A 115 . −5.515 3.549 18.004 1.00 16.13 . 1 858 ATOM N N GLU A 116 . −6.078 8.012 17.584 1.00 14.56 . 1 859 ATOM C CA GLU A 116 . −5.836 9.416 17.859 1.00 14.45 . 1 860 ATOM C C GLU A 116 . −7.080 10.244 17.966 1.00 15.73 . 1 861 ATOM O O GLU A 116 . −7.139 11.168 18.772 1.00 16.57 . 1 862 ATOM C CB GLU A 116 . −4.886 10.005 16.829 1.00 16.28 . 1 863 ATOM C CG GLU A 116 . −3.517 9.326 16.855 1.00 17.98 . 1 864 ATOM C CD GLU A 116 . −2.420 10.139 16.203 1.00 20.45 . 1 865 ATOM O OE1 GLU A 116 . −2.250 10.019 14.974 1.00 19.57 . 1 866 ATOM O OE2 GLU A 116 . −1.729 10.901 16.923 1.00 21.78 . 1 867 ATOM N N CYS A 117 . −8.068 9.963 17.105 1.00 13.99 . 1 868 ATOM C CA CYS A 117 . −9.297 10.706 17.192 1.00 14.66 . 1 869 ATOM C C CYS A 117 . −10.044 10.494 18.526 1.00 14.36 . 1 870 ATOM O O CYS A 117 . −10.412 11.416 19.223 1.00 15.76 . 1 871 ATOM C CB CYS A 117 . −10.220 10.304 16.012 1.00 14.21 . 1 872 ATOM S SG CYS A 117 . −11.905 11.110 16.084 1.00 17.44 . 1 873 ATOM N N VAL A 118 . −10.307 9.247 18.838 1.00 14.33 . 1 874 ATOM C CA VAL A 118 . −11.062 8.915 20.029 1.00 13.79 . 1 875 ATOM C C VAL A 118 . −10.360 9.382 21.306 1.00 14.56 . 1 876 ATOM O O VAL A 118 . −11.011 9.800 22.259 1.00 13.56 . 1 877 ATOM C CB VAL A 118 . −11.262 7.357 20.082 1.00 13.07 . 1 878 ATOM C CG1 VAL A 118 . −11.837 6.887 21.432 1.00 14.53 . 1 879 ATOM C CG2 VAL A 118 . −12.192 6.927 18.948 1.00 15.04 . 1 880 ATOM N N LEU A 119 . −9.032 9.264 21.318 1.00 14.45 . 1 881 ATOM C CA LEU A 119 . −8.329 9.629 22.552 1.00 13.55 . 1 882 ATOM C C LEU A 119 . −7.894 11.067 22.703 1.00 15.08 . 1 883 ATOM O O LEU A 119 . −7.002 11.399 23.462 1.00 14.48 . 1 884 ATOM C CB LEU A 119 . −7.195 8.631 22.831 1.00 13.92 . 1 885 ATOM C CG LEU A 119 . −7.750 7.199 22.972 1.00 13.71 . 1 886 ATOM C CD1 LEU A 119 . −6.603 6.207 23.189 1.00 13.46 . 1 887 ATOM C CD2 LEU A 119 . −8.696 7.100 24.145 1.00 14.91 . 1 888 ATOM N N ASP A 120 . −8.522 11.942 21.924 1.00 13.71 . 1 889 ATOM C CA ASP A 120 . −8.341 13.394 22.061 1.00 13.94 . 1 890 ATOM C C ASP A 120 . −8.711 13.683 23.531 1.00 13.96 . 1 891 ATOM O O ASP A 120 . −9.662 13.131 24.051 1.00 15.43 . 1 892 ATOM C CB ASP A 120 . −9.326 14.143 21.169 1.00 16.74 . 1 893 ATOM C CG ASP A 120 . −9.340 15.605 21.476 1.00 16.60 . 1 894 ATOM O OD1 ASP A 120 . −10.241 16.112 22.175 1.00 18.14 . 1 895 ATOM O OD2 ASP A 120 . −8.426 16.265 20.983 1.00 20.32 . 1 896 ATOM N N PRO A 121 . −7.970 14.550 24.224 1.00 14.29 . 1 897 ATOM C CA PRO A 121 . −8.305 14.797 25.632 1.00 15.14 . 1 898 ATOM C C PRO A 121 . −9.671 15.356 25.908 1.00 16.21 . 1 899 ATOM O O PRO A 121 . −10.292 14.992 26.905 1.00 17.73 . 1 900 ATOM C CB PRO A 121 . −7.196 15.756 26.111 1.00 15.24 . 1 901 ATOM C CG PRO A 121 . −6.034 15.438 25.219 1.00 17.95 . 1 902 ATOM C CD PRO A 121 . −6.699 15.182 23.841 1.00 14.10 . 1 903 ATOM N N THR A 122 . −10.159 16.222 25.032 1.00 15.71 . 1 904 ATOM C CA THR A 122 . −11.466 16.830 25.245 1.00 16.58 . 1 905 ATOM C C THR A 122 . −12.585 15.833 24.982 1.00 16.83 . 1 906 ATOM O O THR A 122 . −13.531 15.714 25.789 1.00 17.46 . 1 907 ATOM C CB THR A 122 . −11.623 18.049 24.356 1.00 17.20 . 1 908 ATOM O OG1 THR A 122 . −10.561 18.967 24.652 1.00 20.20 . 1 909 ATOM C CG2 THR A 122 . −12.952 18.744 24.625 1.00 18.48 . 1 910 ATOM N N LEU A 123 . −12.473 15.080 23.891 1.00 16.71 . 1 911 ATOM C CA LEU A 123 . −13.522 14.116 23.600 1.00 15.69 . 1 912 ATOM C C LEU A 123 . −13.575 12.972 24.608 1.00 14.78 . 1 913 ATOM O O LEU A 123 . −14.608 12.689 25.212 1.00 14.76 . 1 914 ATOM C CB LEU A 123 . −13.410 13.605 22.135 1.00 15.00 . 1 915 ATOM C CG LEU A 123 . −13.432 14.691 21.019 1.00 18.77 . 1 916 ATOM C CD1 LEU A 123 . −13.498 14.029 19.631 1.00 19.08 . 1 917 ATOM C CD2 LEU A 123 . −14.635 15.593 21.201 1.00 17.70 . 1 918 ATOM N N SER A 124 . −12.445 12.312 24.838 1.00 13.83 . 1 919 ATOM C CA SER A 124 . −12.431 11.192 25.775 1.00 14.07 . 1 920 ATOM C C SER A 124 . −12.639 11.661 27.210 1.00 13.80 . 1 921 ATOM O O SER A 124 . −13.257 10.968 28.013 1.00 14.22 . 1 922 ATOM C CB SER A 124 . −11.129 10.377 25.638 1.00 13.74 . 1 923 ATOM O OG SER A 124 . −9.991 11.132 26.015 1.00 15.39 . 1 924 ATOM N N GLY A 125 . −12.142 12.868 27.495 1.00 13.53 . 1 925 ATOM C CA GLY A 125 . −12.344 13.490 28.814 1.00 14.56 . 1 926 ATOM C C GLY A 125 . −13.815 13.761 29.117 1.00 14.18 . 1 927 ATOM O O GLY A 125 . −14.201 13.903 30.297 1.00 14.97 . 1 928 ATOM N N SER A 126 . −14.670 13.822 28.087 1.00 13.58 . 1 929 ATOM C CA SER A 126 . −16.084 14.058 28.295 1.00 14.89 . 1 930 ATOM C C SER A 126 . −16.744 12.967 29.142 1.00 12.78 . 1 931 ATOM O O SER A 126 . −17.771 13.226 29.805 1.00 12.95 . 1 932 ATOM C CB SER A 126 . −16.813 14.085 26.928 1.00 14.74 . 1 933 ATOM O OG SER A 126 . −16.291 15.128 26.155 1.00 19.40 . 1 934 ATOM N N TYR A 127 . −16.114 11.771 29.197 1.00 12.14 . 1 935 ATOM C CA TYR A 127 . −16.733 10.660 29.896 1.00 12.45 . 1 936 ATOM C C TYR A 127 . −16.620 10.813 31.419 1.00 12.70 . 1 937 ATOM O O TYR A 127 . −17.175 10.011 32.144 1.00 13.26 . 1 938 ATOM C CB TYR A 127 . −16.202 9.341 29.349 1.00 12.52 . 1 939 ATOM C CG TYR A 127 . −16.709 9.049 27.927 1.00 12.72 . 1 940 ATOM C CD1 TYR A 127 . −16.182 9.726 26.842 1.00 13.84 . 1 941 ATOM C CD2 TYR A 127 . −17.738 8.124 27.726 1.00 13.76 . 1 942 ATOM C CE1 TYR A 127 . −16.679 9.481 25.541 1.00 12.18 . 1 943 ATOM C CE2 TYR A 127 . −18.272 7.876 26.410 1.00 12.86 . 1 944 ATOM C CZ TYR A 127 . −17.718 8.557 25.349 1.00 12.49 . 1 945 ATOM O OH TYR A 127 . −18.174 8.366 24.038 1.00 13.59 . 1 946 ATOM N N HIS A 128 . −15.890 11.845 31.855 1.00 12.59 . 1 947 ATOM C CA HIS A 128 . −15.854 12.180 33.286 1.00 12.78 . 1 948 ATOM C C HIS A 128 . −17.195 12.759 33.731 1.00 13.63 . 1 949 ATOM O O HIS A 128 . −17.505 12.774 34.945 1.00 15.30 . 1 950 ATOM C CB HIS A 128 . −14.825 13.258 33.551 1.00 14.26 . 1 951 ATOM C CG HIS A 128 . −13.454 12.723 33.665 1.00 14.96 . 1 952 ATOM N ND1 HIS A 128 . −12.978 12.107 34.808 1.00 14.49 . 1 953 ATOM C CD2 HIS A 128 . −12.446 12.687 32.765 1.00 15.69 . 1 954 ATOM C CE1 HIS A 128 . −11.735 11.716 34.602 1.00 14.69 . 1 955 ATOM N NE2 HIS A 128 . −11.387 12.049 33.370 1.00 15.19 . 1 956 ATOM N N GLU A 129 . −18.005 13.190 32.750 1.00 13.39 . 1 957 ATOM C CA GLU A 129 . −19.292 13.820 33.041 1.00 14.10 . 1 958 ATOM C C GLU A 129 . −20.501 12.904 32.782 1.00 12.79 . 1 959 ATOM O O GLU A 129 . −21.606 13.408 32.544 1.00 14.26 . 1 960 ATOM C CB GLU A 129 . −19.438 15.118 32.234 1.00 15.19 . 1 961 ATOM C CG GLU A 129 . −18.359 16.174 32.490 1.00 21.06 . 1 962 ATOM C CD GLU A 129 . −18.195 16.450 33.980 1.00 27.49 . 1 963 ATOM O OE1 GLU A 129 . −19.195 16.883 34.612 1.00 29.07 . 1 964 ATOM O OE2 GLU A 129 . −17.049 16.217 34.503 1.00 32.85 . 1 965 ATOM N N LEU A 130 . −20.322 11.583 32.892 1.00 12.01 . 1 966 ATOM C CA LEU A 130 . −21.462 10.667 32.704 1.00 12.79 . 1 967 ATOM C C LEU A 130 . −22.595 11.036 33.709 1.00 14.32 . 1 968 ATOM O O LEU A 130 . −23.780 11.041 33.309 1.00 14.89 . 1 969 ATOM C CB LEU A 130 . −21.059 9.188 32.870 1.00 13.27 . 1 970 ATOM C CG LEU A 130 . −20.256 8.575 31.713 1.00 11.18 . 1 971 ATOM C CD1 LEU A 130 . −19.716 7.149 32.084 1.00 12.72 . 1 972 ATOM C CD2 LEU A 130 . −21.169 8.534 30.431 1.00 12.35 . 1 973 ATOM N N LYS A 131 . −22.273 11.383 34.968 1.00 13.83 . 1 974 ATOM C CA LYS A 131 . −23.333 11.754 35.948 1.00 13.83 . 1 975 ATOM C C LYS A 131 . −24.154 12.988 35.463 1.00 13.97 . 1 976 ATOM O O LYS A 131 . −25.387 12.938 35.424 1.00 15.34 . 1 977 ATOM C CB LYS A 131 . −22.733 12.039 37.348 1.00 14.13 . 1 978 ATOM C CG LYS A 131 . −23.821 12.504 38.349 1.00 15.01 . 1 979 ATOM C CD LYS A 131 . −23.343 12.347 39.769 1.00 16.97 . 1 980 ATOM C CE LYS A 131 . −24.384 12.888 40.739 1.00 17.72 . 1 981 ATOM N NZ LYS A 131 . −23.736 12.970 42.084 1.00 19.79 . 1 982 ATOM N N LYS A 132 . −23.519 14.095 35.122 1.00 13.57 . 1 983 ATOM C CA LYS A 132 . −24.274 15.264 34.633 1.00 15.17 . 1 984 ATOM C C LYS A 132 . −25.146 14.863 33.420 1.00 13.45 . 1 985 ATOM O O LYS A 132 . −26.301 15.201 33.355 1.00 14.91 . 1 986 ATOM C CB LYS A 132 . −23.323 16.368 34.238 1.00 17.35 . 1 987 ATOM C CG LYS A 132 . −24.050 17.625 33.791 1.00 20.32 . 1 988 ATOM C CD LYS A 132 . −23.124 18.782 33.643 1.00 23.68 . 1 989 ATOM C CE LYS A 132 . −23.903 20.077 33.453 1.00 27.63 . 1 990 ATOM N NZ LYS A 132 . −23.008 21.255 33.138 1.00 29.76 . 1 991 ATOM N N TRP A 133 . −24.574 14.071 32.512 1.00 13.36 . 1 992 ATOM C CA TRP A 133 . −25.299 13.648 31.318 1.00 13.06 . 1 993 ATOM C C TRP A 133 . −26.497 12.752 31.618 1.00 13.71 . 1 994 ATOM O O TRP A 133 . −27.568 12.861 30.971 1.00 13.92 . 1 995 ATOM C CB TRP A 133 . −24.288 12.909 30.397 1.00 12.94 . 1 996 ATOM C CG TRP A 133 . −24.944 12.149 29.261 1.00 12.87 . 1 997 ATOM C CD1 TRP A 133 . −25.588 12.669 28.144 1.00 14.70 . 1 998 ATOM C CD2 TRP A 133 . −25.063 10.738 29.191 1.00 11.03 . 1 999 ATOM N NE1 TRP A 133 . −26.104 11.610 27.404 1.00 14.23 . 1 1000 ATOM C CE2 TRP A 133 . −25.790 10.424 28.021 1.00 11.75 . 1 1001 ATOM C CE3 TRP A 133 . −24.633 9.693 30.004 1.00 13.00 . 1 1002 ATOM C CZ2 TRP A 133 . −26.064 9.103 27.654 1.00 12.58 . 1 1003 ATOM C CZ3 TRP A 133 . −24.900 8.395 29.646 1.00 12.39 . 1 1004 ATOM C CH2 TRP A 133 . −25.607 8.100 28.482 1.00 13.06 . 1 1005 ATOM N N ILE A 134 . −26.372 11.853 32.578 1.00 13.14 . 1 1006 ATOM C CA ILE A 134 . −27.490 10.927 32.852 1.00 15.06 . 1 1007 ATOM C C ILE A 134 . −28.683 11.720 33.413 1.00 16.15 . 1 1008 ATOM O O ILE A 134 . −29.815 11.249 33.354 1.00 16.30 . 1 1009 ATOM C CB ILE A 134 . −27.071 9.749 33.805 1.00 15.44 . 1 1010 ATOM C CG1 ILE A 134 . −27.976 8.546 33.548 1.00 17.34 . 1 1011 ATOM C CG2 ILE A 134 . −27.049 10.186 35.292 1.00 17.40 . 1 1012 ATOM C CD1 ILE A 134 . −27.527 7.747 32.308 1.00 16.84 . 1 1013 ATOM N N TYR A 135 . −28.420 12.931 33.918 1.00 15.04 . 1 1014 ATOM C CA TYR A 135 . −29.498 13.779 34.441 1.00 15.07 . 1 1015 ATOM C C TYR A 135 . −30.069 14.734 33.411 1.00 17.99 . 1 1016 ATOM O O TYR A 135 . −31.022 15.487 33.710 1.00 18.51 . 1 1017 ATOM C CB TYR A 135 . −29.055 14.529 35.718 1.00 15.37 . 1 1018 ATOM C CG TYR A 135 . −29.118 13.602 36.910 1.00 15.25 . 1 1019 ATOM C CD1 TYR A 135 . −27.971 13.025 37.460 1.00 15.67 . 1 1020 ATOM C CD2 TYR A 135 . −30.349 13.254 37.472 1.00 15.42 . 1 1021 ATOM C CE1 TYR A 135 . −28.041 12.124 38.527 1.00 15.58 . 1 1022 ATOM C CE2 TYR A 135 . −30.439 12.355 38.530 1.00 16.23 . 1 1023 ATOM C CZ TYR A 135 . −29.272 11.782 39.064 1.00 17.55 . 1 1024 ATOM O OH TYR A 135 . −29.324 10.853 40.084 1.00 18.86 . 1 1025 ATOM N N GLU A 136 . −29.518 14.737 32.202 1.00 16.48 . 1 1026 ATOM C CA GLU A 136 . −30.021 15.633 31.155 1.00 17.94 . 1 1027 ATOM C C GLU A 136 . −31.147 14.948 30.381 1.00 18.24 . 1 1028 ATOM O O GLU A 136 . −30.994 13.847 29.895 1.00 18.07 . 1 1029 ATOM C CB GLU A 136 . −28.877 15.987 30.184 1.00 17.69 . 1 1030 ATOM C CG GLU A 136 . −27.865 16.972 30.728 1.00 21.00 . 1 1031 ATOM C CD GLU A 136 . −28.466 18.294 31.136 1.00 22.49 . 1 1032 ATOM O OE1 GLU A 136 . −29.431 18.785 30.488 1.00 21.66 . 1 1033 ATOM O OE2 GLU A 136 . −27.939 18.864 32.134 1.00 25.56 . 1 1034 ATOM N N GLU A 137 . −32.289 15.616 30.243 1.00 19.63 . 1 1035 ATOM C CA GLU A 137 . −33.381 15.009 29.490 1.00 19.80 . 1 1036 ATOM C C GLU A 137 . −33.050 14.851 28.016 1.00 20.69 . 1 1037 ATOM O O GLU A 137 . −33.435 13.862 27.408 1.00 21.70 . 1 1038 ATOM C CB GLU A 137 . −34.602 15.886 29.470 1.00 25.53 . 1 1039 ATOM C CG GLU A 137 . −35.241 16.279 30.726 1.00 31.95 . 1 1040 ATOM C CD GLU A 137 . −36.379 17.224 30.391 1.00 36.12 . 1 1041 ATOM O OE1 GLU A 137 . −37.298 16.784 29.652 1.00 37.59 . 1 1042 ATOM O OE2 GLU A 137 . −36.338 18.404 30.831 1.00 39.01 . 1 1043 ATOM N N ASP A 138 . −32.388 15.844 27.442 1.00 18.97 . 1 1044 ATOM C CA ASP A 138 . −32.100 15.820 26.016 1.00 19.85 . 1 1045 ATOM C C ASP A 138 . −30.654 15.825 25.532 1.00 18.83 . 1 1046 ATOM O O ASP A 138 . −30.373 15.227 24.489 1.00 18.96 . 1 1047 ATOM C CB ASP A 138 . −32.788 17.007 25.327 1.00 23.36 . 1 1048 ATOM C CG ASP A 138 . −34.292 17.109 25.651 1.00 27.38 . 1 1049 ATOM O OD1 ASP A 138 . −35.067 16.165 25.354 1.00 30.11 . 1 1050 ATOM O OD2 ASP A 138 . −34.689 18.154 26.226 1.00 30.89 . 1 1051 ATOM N N LEU A 139 . −29.749 16.494 26.234 1.00 17.53 . 1 1052 ATOM C CA LEU A 139 . −28.384 16.618 25.757 1.00 16.59 . 1 1053 ATOM C C LEU A 139 . −27.679 15.271 25.606 1.00 14.32 . 1 1054 ATOM O O LEU A 139 . −27.939 14.325 26.353 1.00 14.93 . 1 1055 ATOM C CB LEU A 139 . −27.575 17.534 26.712 1.00 18.62 . 1 1056 ATOM C CG LEU A 139 . −27.931 19.009 26.821 1.00 19.40 . 1 1057 ATOM C CD1 LEU A 139 . −26.968 19.653 27.797 1.00 22.40 . 1 1058 ATOM C CD2 LEU A 139 . −27.822 19.679 25.450 1.00 20.91 . 1 1059 ATOM N N THR A 140 . −26.809 15.214 24.612 1.00 15.85 . 1 1060 ATOM C CA THR A 140 . −25.947 14.032 24.392 1.00 14.74 . 1 1061 ATOM C C THR A 140 . −24.741 14.282 25.320 1.00 16.70 . 1 1062 ATOM O O THR A 140 . −24.593 15.414 25.812 1.00 17.06 . 1 1063 ATOM C CB THR A 140 . −25.388 14.005 22.950 1.00 16.44 . 1 1064 ATOM O OG1 THR A 140 . −24.656 15.218 22.716 1.00 16.82 . 1 1065 ATOM C CG2 THR A 140 . −26.532 13.818 21.913 1.00 15.44 . 1 1066 ATOM N N LEU A 141 . −23.891 13.263 25.537 1.00 14.95 . 1 1067 ATOM C CA LEU A 141 . −22.717 13.495 26.384 1.00 15.62 . 1 1068 ATOM C C LEU A 141 . −21.830 14.587 25.771 1.00 17.60 . 1 1069 ATOM O O LEU A 141 . −21.338 15.464 26.463 1.00 17.72 . 1 1070 ATOM C CB LEU A 141 . −21.970 12.186 26.594 1.00 13.50 . 1 1071 ATOM C CG LEU A 141 . −20.630 12.290 27.386 1.00 14.03 . 1 1072 ATOM C CD1 LEU A 141 . −20.962 12.658 28.876 1.00 16.41 . 1 1073 ATOM C CD2 LEU A 141 . −19.999 10.917 27.392 1.00 17.25 . 1 1074 ATOM N N PHE A 142 . −21.548 14.526 24.470 1.00 15.39 . 1 1075 ATOM C CA PHE A 142 . −20.751 15.593 23.897 1.00 16.57 . 1 1076 ATOM C C PHE A 142 . −21.441 16.949 24.005 1.00 18.71 . 1 1077 ATOM O O PHE A 142 . −20.778 17.970 24.119 1.00 21.09 . 1 1078 ATOM C CB PHE A 142 . −20.370 15.305 22.417 1.00 15.89 . 1 1079 ATOM C CG PHE A 142 . −19.273 14.294 22.244 1.00 15.62 . 1 1080 ATOM C CD1 PHE A 142 . −18.952 13.812 20.969 1.00 17.38 . 1 1081 ATOM C CD2 PHE A 142 . −18.532 13.828 23.334 1.00 17.34 . 1 1082 ATOM C CE1 PHE A 142 . −17.927 12.899 20.770 1.00 19.06 . 1 1083 ATOM C CE2 PHE A 142 . −17.492 12.896 23.139 1.00 16.90 . 1 1084 ATOM C CZ PHE A 142 . −17.191 12.435 21.876 1.00 18.12 . 1 1085 ATOM N N GLY A 143 . −22.766 16.980 23.954 1.00 18.95 . 1 1086 ATOM C CA GLY A 143 . −23.491 18.243 24.066 1.00 18.90 . 1 1087 ATOM C C GLY A 143 . −23.261 18.911 25.431 1.00 20.25 . 1 1088 ATOM O O GLY A 143 . −23.197 20.148 25.546 1.00 20.67 . 1 1089 ATOM N N VAL A 144 . −23.158 18.085 26.454 1.00 18.44 . 1 1090 ATOM C CA VAL A 144 . −22.880 18.544 27.804 1.00 18.86 . 1 1091 ATOM C C VAL A 144 . −21.487 19.149 27.931 1.00 19.68 . 1 1092 ATOM O O VAL A 144 . −21.325 20.182 28.581 1.00 21.38 . 1 1093 ATOM C CB VAL A 144 . −22.945 17.362 28.788 1.00 17.65 . 1 1094 ATOM C CG1 VAL A 144 . −22.340 17.812 30.186 1.00 19.45 . 1 1095 ATOM C CG2 VAL A 144 . −24.370 16.956 28.999 1.00 18.75 . 1 1096 ATOM N N THR A 145 . −20.484 18.527 27.302 1.00 18.11 . 1 1097 ATOM C CA THR A 145 . −19.097 18.947 27.467 1.00 18.79 . 1 1098 ATOM C C THR A 145 . −18.563 19.920 26.446 1.00 18.48 . 1 1099 ATOM O O THR A 145 . −17.713 20.723 26.767 1.00 20.32 . 1 1100 ATOM C CB THR A 145 . −18.183 17.710 27.499 1.00 19.06 . 1 1101 ATOM O OG1 THR A 145 . −18.377 16.968 26.288 1.00 20.60 . 1 1102 ATOM C CG2 THR A 145 . −18.560 16.789 28.644 1.00 20.20 . 1 1103 ATOM N N LEU A 146 . −19.073 19.886 25.215 1.00 17.19 . 1 1104 ATOM C CA LEU A 146 . −18.564 20.769 24.169 1.00 19.36 . 1 1105 ATOM C C LEU A 146 . −19.372 22.031 24.074 1.00 21.56 . 1 1106 ATOM O O LEU A 146 . −18.918 22.981 23.447 1.00 25.25 . 1 1107 ATOM C CB LEU A 146 . −18.569 20.056 22.796 1.00 18.53 . 1 1108 ATOM C CG LEU A 146 . −17.861 18.702 22.709 1.00 16.94 . 1 1109 ATOM C CD1 LEU A 146 . −17.892 18.127 21.273 1.00 20.94 . 1 1110 ATOM C CD2 LEU A 146 . −16.371 18.847 23.208 1.00 21.75 . 1 1111 ATOM N N GLY A 147 . −20.571 22.055 24.630 1.00 23.60 . 1 1112 ATOM C CA GLY A 147 . −21.336 23.310 24.546 1.00 24.43 . 1 1113 ATOM C C GLY A 147 . −22.128 23.492 23.262 1.00 25.12 . 1 1114 ATOM O O GLY A 147 . −22.737 24.563 23.030 1.00 26.00 . 1 1115 ATOM N N SER A 148 . −22.089 22.494 22.391 1.00 22.56 . 1 1116 ATOM C CA SER A 148 . −22.895 22.550 21.173 1.00 21.73 . 1 1117 ATOM C C SER A 148 . −23.004 21.130 20.751 1.00 21.66 . 1 1118 ATOM O O SER A 148 . −22.340 20.278 21.333 1.00 22.19 . 1 1119 ATOM C CB SER A 148 . −22.227 23.358 20.058 1.00 22.47 . 1 1120 ATOM O OG SER A 148 . −21.216 22.633 19.366 1.00 21.53 . 1 1121 ATOM N N GLY A 149 . −23.836 20.864 19.747 1.00 20.64 . 1 1122 ATOM C CA GLY A 149 . −23.947 19.484 19.273 1.00 21.12 . 1 1123 ATOM C C GLY A 149 . −22.646 19.143 18.560 1.00 19.68 . 1 1124 ATOM O O GLY A 149 . −21.923 20.070 18.126 1.00 19.22 . 1 1125 ATOM N N PHE A 150 . −22.362 17.848 18.390 1.00 19.27 . 1 1126 ATOM C CA PHE A 150 . −21.121 17.401 17.760 1.00 17.55 . 1 1127 ATOM C C PHE A 150 . −20.888 17.905 16.313 1.00 18.11 . 1 1128 ATOM O O PHE A 150 . −19.790 18.299 15.964 1.00 16.51 . 1 1129 ATOM C CB PHE A 150 . −21.040 15.867 17.797 1.00 17.81 . 1 1130 ATOM C CG PHE A 150 . −19.731 15.299 17.334 1.00 16.11 . 1 1131 ATOM C CD1 PHE A 150 . −18.539 15.570 18.024 1.00 14.95 . 1 1132 ATOM C CD2 PHE A 150 . −19.667 14.446 16.226 1.00 15.89 . 1 1133 ATOM C CE1 PHE A 150 . −17.353 15.022 17.651 1.00 15.41 . 1 1134 ATOM C CE2 PHE A 150 . −18.475 13.873 15.830 1.00 16.43 . 1 1135 ATOM C CZ PHE A 150 . −17.291 14.150 16.538 1.00 17.66 . 1 1136 ATOM N N TRP A 151 . −21.908 17.861 15.464 1.00 17.66 . 1 1137 ATOM C CA TRP A 151 . −21.659 18.273 14.099 1.00 17.55 . 1 1138 ATOM C C TRP A 151 . −21.356 19.758 13.992 1.00 18.58 . 1 1139 ATOM O O TRP A 151 . −20.468 20.140 13.247 1.00 19.77 . 1 1140 ATOM C CB TRP A 151 . −22.851 17.841 13.200 1.00 17.66 . 1 1141 ATOM C CG TRP A 151 . −23.224 16.374 13.437 1.00 15.36 . 1 1142 ATOM C CD1 TRP A 151 . −24.338 15.902 14.061 1.00 17.26 . 1 1143 ATOM C CD2 TRP A 151 . −22.383 15.220 13.208 1.00 16.37 . 1 1144 ATOM N NE1 TRP A 151 . −24.240 14.539 14.261 1.00 17.96 . 1 1145 ATOM C CE2 TRP A 151 . −23.049 14.094 13.749 1.00 16.49 . 1 1146 ATOM C CE3 TRP A 151 . −21.121 15.050 12.616 1.00 16.64 . 1 1147 ATOM C CZ2 TRP A 151 . −22.473 12.782 13.715 1.00 14.01 . 1 1148 ATOM C CZ3 TRP A 151 . −20.556 13.789 12.588 1.00 16.25 . 1 1149 ATOM C CH2 TRP A 151 . −21.233 12.670 13.139 1.00 17.42 . 1 1150 ATOM N N ASP A 152 . −22.093 20.582 14.742 1.00 20.05 . 1 1151 ATOM C CA ASP A 152 . −21.811 22.006 14.763 1.00 21.85 . 1 1152 ATOM C C ASP A 152 . −20.392 22.218 15.262 1.00 20.40 . 1 1153 ATOM O O ASP A 152 . −19.658 23.083 14.743 1.00 22.74 . 1 1154 ATOM C CB ASP A 152 . −22.769 22.735 15.692 1.00 23.69 . 1 1155 ATOM C CG ASP A 152 . −24.218 22.789 15.134 1.00 27.64 . 1 1156 ATOM O OD1 ASP A 152 . −24.434 22.629 13.901 1.00 28.56 . 1 1157 ATOM O OD2 ASP A 152 . −25.161 23.019 15.942 1.00 29.23 . 1 1158 ATOM N N PHE A 153 . −20.025 21.459 16.297 1.00 18.41 . 1 1159 ATOM C CA PHE A 153 . −18.673 21.531 16.857 1.00 18.96 . 1 1160 ATOM C C PHE A 153 . −17.621 21.250 15.756 1.00 18.69 . 1 1161 ATOM O O PHE A 153 . −16.634 21.994 15.608 1.00 19.51 . 1 1162 ATOM C CB PHE A 153 . −18.524 20.490 18.016 1.00 18.65 . 1 1163 ATOM C CG PHE A 153 . −17.140 20.402 18.590 1.00 20.69 . 1 1164 ATOM C CD1 PHE A 153 . −16.677 21.371 19.492 1.00 22.80 . 1 1165 ATOM C CD2 PHE A 153 . −16.301 19.367 18.204 1.00 21.70 . 1 1166 ATOM C CE1 PHE A 153 . −15.409 21.306 19.987 1.00 23.62 . 1 1167 ATOM C CE2 PHE A 153 . −15.020 19.292 18.701 1.00 24.03 . 1 1168 ATOM C CZ PHE A 153 . −14.570 20.266 19.595 1.00 23.63 . 1 1169 ATOM N N LEU A 154 . −17.826 20.204 14.945 1.00 16.71 . 1 1170 ATOM C CA LEU A 154 . −16.826 19.915 13.921 1.00 17.29 . 1 1171 ATOM C C LEU A 154 . −16.740 21.084 12.921 1.00 17.72 . 1 1172 ATOM O O LEU A 154 . −15.679 21.401 12.413 1.00 18.83 . 1 1173 ATOM C CB LEU A 154 . −17.195 18.619 13.188 1.00 18.47 . 1 1174 ATOM C CG LEU A 154 . −17.113 17.311 14.008 1.00 17.43 . 1 1175 ATOM C CD1 LEU A 154 . −17.370 16.136 13.056 1.00 16.06 . 1 1176 ATOM C CD2 LEU A 154 . −15.724 17.128 14.643 1.00 16.94 . 1 1177 ATOM N N ASP A 155 . −17.872 21.720 12.655 1.00 19.57 . 1 1178 ATOM C CA ASP A 155 . −17.854 22.810 11.668 1.00 20.56 . 1 1179 ATOM C C ASP A 155 . −17.027 23.992 12.118 1.00 21.25 . 1 1180 ATOM O O ASP A 155 . −16.454 24.711 11.282 1.00 23.17 . 1 1181 ATOM C CB ASP A 155 . −19.271 23.314 11.359 1.00 21.38 . 1 1182 ATOM C CG ASP A 155 . −20.099 22.324 10.551 1.00 21.28 . 1 1183 ATOM O OD1 ASP A 155 . −19.552 21.377 9.952 1.00 21.00 . 1 1184 ATOM O OD2 ASP A 155 . −21.341 22.543 10.507 1.00 23.81 . 1 1185 ATOM N N LYS A 156 . −16.964 24.185 13.436 1.00 20.79 . 1 1186 ATOM C CA LYS A 156 . −16.223 25.297 14.048 1.00 21.98 . 1 1187 ATOM C C LYS A 156 . −14.776 24.983 14.411 1.00 22.27 . 1 1188 ATOM O O LYS A 156 . −13.994 25.892 14.771 1.00 22.56 . 1 1189 ATOM C CB LYS A 156 . −16.947 25.752 15.312 1.00 22.79 . 1 1190 ATOM C CG LYS A 156 . −18.277 26.423 15.033 1.00 27.51 . 1 1191 ATOM C CD LYS A 156 . −19.033 26.682 16.306 1.00 32.29 . 1 1192 ATOM C CE LYS A 156 . −20.235 27.585 16.024 1.00 34.06 . 1 1193 ATOM N NZ LYS A 156 . −20.303 28.693 17.037 1.00 37.21 . 1 1194 ATOM N N ASN A 157 . −14.398 23.710 14.315 1.00 20.49 . 1 1195 ATOM C CA ASN A 157 . −13.072 23.293 14.742 1.00 20.59 . 1 1196 ATOM C C ASN A 157 . −12.434 22.413 13.676 1.00 21.18 . 1 1197 ATOM O O ASN A 157 . −12.484 21.193 13.756 1.00 20.56 . 1 1198 ATOM C CB ASN A 157 . −13.236 22.545 16.071 1.00 21.21 . 1 1199 ATOM C CG ASN A 157 . −13.688 23.465 17.204 1.00 21.46 . 1 1200 ATOM O OD1 ASN A 157 . −12.856 24.137 17.827 1.00 24.11 . 1 1201 ATOM N ND2 ASN A 157 . −14.997 23.521 17.477 1.00 20.18 . 1 1202 ATOM N N PRO A 158 . −11.818 23.026 12.666 1.00 21.08 . 1 1203 ATOM C CA PRO A 158 . −11.185 22.308 11.572 1.00 21.76 . 1 1204 ATOM C C PRO A 158 . −10.303 21.140 11.938 1.00 21.17 . 1 1205 ATOM O O PRO A 158 . −10.369 20.081 11.303 1.00 21.18 . 1 1206 ATOM C CB PRO A 158 . −10.410 23.420 10.820 1.00 23.21 . 1 1207 ATOM C CG PRO A 158 . −11.239 24.605 11.044 1.00 24.10 . 1 1208 ATOM C CD PRO A 158 . −11.607 24.486 12.510 1.00 20.86 . 1 1209 ATOM N N GLU A 159 . −9.436 21.312 12.929 1.00 21.23 . 1 1210 ATOM C CA GLU A 159 . −8.559 20.210 13.286 1.00 21.78 . 1 1211 ATOM C C GLU A 159 . −9.355 19.009 13.794 1.00 20.27 . 1 1212 ATOM O O GLU A 159 . −8.956 17.849 13.575 1.00 19.51 . 1 1213 ATOM C CB GLU A 159 . −7.546 20.665 14.329 1.00 25.11 . 1 1214 ATOM C CG GLU A 159 . −6.490 21.604 13.763 1.00 31.67 . 1 1215 ATOM C CD GLU A 159 . −5.599 22.221 14.864 1.00 35.82 . 1 1216 ATOM O OE1 GLU A 159 . −4.684 21.510 15.358 1.00 37.63 . 1 1217 ATOM O OE2 GLU A 159 . −5.820 23.415 15.245 1.00 38.53 . 1 1218 ATOM N N TYR A 160 . −10.467 19.287 14.473 1.00 18.85 . 1 1219 ATOM C CA TYR A 160 . −11.291 18.189 14.965 1.00 19.00 . 1 1220 ATOM C C TYR A 160 . −12.028 17.535 13.786 1.00 18.41 . 1 1221 ATOM O O TYR A 160 . −12.227 16.312 13.769 1.00 18.67 . 1 1222 ATOM C CB TYR A 160 . −12.318 18.656 16.014 1.00 18.95 . 1 1223 ATOM C CG TYR A 160 . −11.746 18.721 17.404 1.00 21.28 . 1 1224 ATOM C CD1 TYR A 160 . −11.098 19.858 17.861 1.00 22.35 . 1 1225 ATOM C CD2 TYR A 160 . −11.864 17.649 18.269 1.00 20.75 . 1 1226 ATOM C CE1 TYR A 160 . −10.574 19.923 19.172 1.00 22.69 . 1 1227 ATOM C CE2 TYR A 160 . −11.351 17.700 19.567 1.00 21.70 . 1 1228 ATOM C CZ TYR A 160 . −10.713 18.819 20.019 1.00 22.89 . 1 1229 ATOM O OH TYR A 160 . −10.208 18.812 21.333 1.00 22.81 . 1 1230 ATOM N N ASN A 161 . −12.446 18.353 12.829 1.00 18.40 . 1 1231 ATOM C CA ASN A 161 . −13.128 17.809 11.667 1.00 17.78 . 1 1232 ATOM C C ASN A 161 . −12.158 16.904 10.875 1.00 16.78 . 1 1233 ATOM O O ASN A 161 . −12.520 15.808 10.432 1.00 16.06 . 1 1234 ATOM C CB ASN A 161 . −13.595 18.956 10.800 1.00 18.96 . 1 1235 ATOM C CG ASN A 161 . −14.507 18.507 9.712 1.00 17.55 . 1 1236 ATOM O OD1 ASN A 161 . −15.577 17.967 9.972 1.00 20.17 . 1 1237 ATOM N ND2 ASN A 161 . −14.088 18.718 8.473 1.00 20.45 . 1 1238 ATOM N N THR A 162 . −10.906 17.312 10.727 1.00 17.76 . 1 1239 ATOM C CA THR A 162 . −9.921 16.533 10.020 1.00 18.28 . 1 1240 ATOM C C THR A 162 . −9.676 15.213 10.743 1.00 18.72 . 1 1241 ATOM O O THR A 162 . −9.662 14.131 10.134 1.00 20.55 . 1 1242 ATOM C CB THR A 162 . −8.606 17.333 9.911 1.00 20.46 . 1 1243 ATOM O OG1 THR A 162 . −8.836 18.477 9.083 1.00 22.55 . 1 1244 ATOM C CG2 THR A 162 . −7.462 16.469 9.294 1.00 21.64 . 1 1245 ATOM N N SER A 163 . −9.477 15.286 12.052 1.00 19.18 . 1 1246 ATOM C CA SER A 163 . −9.240 14.097 12.828 1.00 17.84 . 1 1247 ATOM C C SER A 163 . −10.417 13.083 12.720 1.00 15.92 . 1 1248 ATOM O O SER A 163 . −10.214 11.878 12.517 1.00 16.00 . 1 1249 ATOM C CB SER A 163 . −9.039 14.538 14.260 1.00 20.74 . 1 1250 ATOM O OG SER A 163 . −8.842 13.417 15.048 1.00 25.67 . 1 1251 ATOM N N PHE A 164 . −11.644 13.598 12.821 1.00 15.19 . 1 1252 ATOM C CA PHE A 164 . −12.826 12.754 12.696 1.00 13.72 . 1 1253 ATOM C C PHE A 164 . −12.887 12.162 11.272 1.00 16.53 . 1 1254 ATOM O O PHE A 164 . −13.153 10.976 11.130 1.00 14.51 . 1 1255 ATOM C CB PHE A 164 . −14.112 13.562 12.959 1.00 17.07 . 1 1256 ATOM C CG PHE A 164 . −15.366 12.735 12.851 1.00 17.74 . 1 1257 ATOM C CD1 PHE A 164 . −15.662 11.804 13.842 1.00 18.65 . 1 1258 ATOM C CD2 PHE A 164 . −16.201 12.845 11.754 1.00 20.13 . 1 1259 ATOM C CE1 PHE A 164 . −16.811 10.969 13.739 1.00 19.27 . 1 1260 ATOM C CE2 PHE A 164 . −17.338 12.037 11.633 1.00 19.40 . 1 1261 ATOM C CZ PHE A 164 . −17.634 11.114 12.620 1.00 19.38 . 1 1262 ATOM N N ASN A 165 . −12.658 12.964 10.232 1.00 17.17 . 1 1263 ATOM C CA ASN A 165 . −12.712 12.400 8.883 1.00 18.28 . 1 1264 ATOM C C ASN A 165 . −11.664 11.344 8.657 1.00 17.89 . 1 1265 ATOM O O ASN A 165 . −11.950 10.329 7.986 1.00 19.65 . 1 1266 ATOM C CB ASN A 165 . −12.494 13.461 7.810 1.00 19.43 . 1 1267 ATOM C CG ASN A 165 . −13.664 14.411 7.677 1.00 22.08 . 1 1268 ATOM O OD1 ASN A 165 . −14.795 14.109 8.050 1.00 26.04 . 1 1269 ATOM N ND2 ASN A 165 . −13.383 15.595 7.130 1.00 25.08 . 1 1270 ATOM N N ASP A 166 . −10.457 11.570 9.166 1.00 17.98 . 1 1271 ATOM C CA ASP A 166 . −9.398 10.572 8.998 1.00 16.43 . 1 1272 ATOM C C ASP A 166 . −9.776 9.276 9.738 1.00 17.50 . 1 1273 ATOM O O ASP A 166 . −9.491 8.160 9.272 1.00 17.73 . 1 1274 ATOM C CB ASP A 166 . −8.039 11.045 9.541 1.00 18.76 . 1 1275 ATOM C CG ASP A 166 . −7.402 12.136 8.697 1.00 22.09 . 1 1276 ATOM O OD1 ASP A 166 . −7.818 12.312 7.558 1.00 23.98 . 1 1277 ATOM O OD2 ASP A 166 . −6.472 12.789 9.199 1.00 23.70 . 1 1278 ATOM N N ALA A 167 . −10.402 9.429 10.888 1.00 15.89 . 1 1279 ATOM C CA ALA A 167 . −10.806 8.259 11.661 1.00 16.35 . 1 1280 ATOM C C ALA A 167 . −11.881 7.496 10.861 1.00 17.59 . 1 1281 ATOM O O ALA A 167 . −11.784 6.305 10.743 1.00 18.01 . 1 1282 ATOM C CB ALA A 167 . −11.328 8.667 13.022 1.00 17.62 . 1 1283 ATOM N N MET A 168 . −12.902 8.196 10.351 1.00 16.65 . 1 1284 ATOM C CA MET A 168 . −13.927 7.500 9.550 1.00 18.06 . 1 1285 ATOM C C MET A 168 . −13.307 6.872 8.303 1.00 17.13 . 1 1286 ATOM O O MET A 168 . −13.737 5.797 7.863 1.00 18.54 . 1 1287 ATOM C CB MET A 168 . −15.020 8.493 9.140 1.00 18.72 . 1 1288 ATOM C CG MET A 168 . −15.908 8.969 10.293 1.00 21.36 . 1 1289 ATOM S SD MET A 168 . −16.550 7.712 11.365 1.00 21.68 . 1 1290 ATOM C CE MET A 168 . −17.548 6.821 10.169 1.00 19.56 . 1 1291 ATOM N N ALA A 169 . −12.299 7.493 7.715 1.00 14.93 . 1 1292 ATOM C CA ALA A 169 . −11.696 6.928 6.517 1.00 16.38 . 1 1293 ATOM C C ALA A 169 . −10.913 5.661 6.775 1.00 17.37 . 1 1294 ATOM O O ALA A 169 . −10.807 4.818 5.916 1.00 18.41 . 1 1295 ATOM C CB ALA A 169 . −10.731 7.944 5.875 1.00 16.88 . 1 1296 ATOM N N SER A 170 . −10.375 5.545 7.985 1.00 17.91 . 1 1297 ATOM C CA SER A 170 . −9.498 4.432 8.330 1.00 18.87 . 1 1298 ATOM C C SER A 170 . −10.035 3.010 8.098 1.00 18.70 . 1 1299 ATOM O O SER A 170 . −9.290 2.139 7.714 1.00 18.96 . 1 1300 ATOM C CB SER A 170 . −8.972 4.638 9.780 1.00 18.39 . 1 1301 ATOM O OG SER A 170 . −10.008 4.372 10.706 1.00 21.39 . 1 1302 ATOM N N ASP A 171 . −11.314 2.741 8.321 1.00 20.49 . 1 1303 ATOM C CA ASP A 171 . −11.792 1.376 7.968 1.00 19.77 . 1 1304 ATOM C C ASP A 171 . −12.691 1.482 6.722 1.00 20.78 . 1 1305 ATOM O O ASP A 171 . −13.340 0.520 6.337 1.00 19.37 . 1 1306 ATOM C CB ASP A 171 . −12.600 0.695 9.094 1.00 21.69 . 1 1307 ATOM C CG ASP A 171 . −13.820 1.483 9.530 1.00 20.87 . 1 1308 ATOM O OD1 ASP A 171 . −14.093 2.586 8.996 1.00 20.45 . 1 1309 ATOM O OD2 ASP A 171 . −14.498 0.991 10.456 1.00 21.56 . 1 1310 ATOM N N SER A 172 . −12.658 2.607 6.033 1.00 19.35 . 1 1311 ATOM C CA SER A 172 . −13.555 2.735 4.888 1.00 19.85 . 1 1312 ATOM C C SER A 172 . −13.333 1.808 3.722 1.00 21.52 . 1 1313 ATOM O O SER A 172 . −14.309 1.303 3.165 1.00 21.70 . 1 1314 ATOM C CB SER A 172 . −13.607 4.167 4.381 1.00 17.59 . 1 1315 ATOM O OG SER A 172 . −12.432 4.591 3.752 1.00 19.13 . 1 1316 ATOM N N LYS A 173 . −12.071 1.591 3.329 1.00 21.73 . 1 1317 ATOM C CA LYS A 173 . −11.822 0.717 2.167 1.00 23.09 . 1 1318 ATOM C C LYS A 173 . −12.446 −0.668 2.368 1.00 21.00 . 1 1319 ATOM O O LYS A 173 . −13.096 −1.177 1.484 1.00 20.98 . 1 1320 ATOM C CB LYS A 173 . −10.310 0.528 1.932 1.00 25.45 . 1 1321 ATOM C CG LYS A 173 . −9.487 1.780 1.635 1.00 31.65 . 1 1322 ATOM C CD LYS A 173 . −7.952 1.442 1.566 1.00 35.17 . 1 1323 ATOM C CE LYS A 173 . −7.073 2.696 1.353 1.00 36.84 . 1 1324 ATOM N NZ LYS A 173 . −7.261 3.263 −0.022 1.00 37.81 . 1 1325 ATOM N N LEU A 174 . −12.221 −1.260 3.532 1.00 20.33 . 1 1326 ATOM C CA LEU A 174 . −12.733 −2.584 3.855 1.00 21.12 . 1 1327 ATOM C C LEU A 174 . −14.268 −2.706 3.756 1.00 19.90 . 1 1328 ATOM O O LEU A 174 . −14.835 −3.655 3.197 1.00 19.37 . 1 1329 ATOM C CB LEU A 174 . −12.338 −2.925 5.281 1.00 23.63 . 1 1330 ATOM C CG LEU A 174 . −11.415 −4.128 5.556 1.00 26.75 . 1 1331 ATOM C CD1 LEU A 174 . −11.520 −4.565 7.020 1.00 24.60 . 1 1332 ATOM C CD2 LEU A 174 . −11.754 −5.275 4.632 1.00 26.45 . 1 1333 ATOM N N ILE A 175 . −14.946 −1.727 4.335 1.00 17.33 . 1 1334 ATOM C CA ILE A 175 . −16.407 −1.741 4.356 1.00 16.73 . 1 1335 ATOM C C ILE A 175 . −16.934 −1.419 2.975 1.00 14.05 . 1 1336 ATOM O O ILE A 175 . −17.873 −2.080 2.522 1.00 14.32 . 1 1337 ATOM C CB ILE A 175 . −16.940 −0.671 5.348 1.00 15.75 . 1 1338 ATOM C CG1 ILE A 175 . −16.362 −0.942 6.729 1.00 17.12 . 1 1339 ATOM C CG2 ILE A 175 . −18.538 −0.603 5.352 1.00 15.16 . 1 1340 ATOM C CD1 ILE A 175 . −16.539 0.300 7.654 1.00 16.58 . 1 1341 ATOM N N ASN A 176 . −16.336 −0.428 2.325 1.00 14.23 . 1 1342 ATOM C CA ASN A 176 . −16.842 −0.011 1.032 1.00 13.63 . 1 1343 ATOM C C ASN A 176 . −16.624 −1.091 −0.012 1.00 14.57 . 1 1344 ATOM O O ASN A 176 . −17.479 −1.287 −0.868 1.00 15.36 . 1 1345 ATOM C CB ASN A 176 . −16.228 1.333 0.582 1.00 14.61 . 1 1346 ATOM C CG ASN A 176 . −16.672 2.512 1.453 1.00 14.35 . 1 1347 ATOM O OD1 ASN A 176 . −17.771 2.514 2.008 1.00 14.75 . 1 1348 ATOM N ND2 ASN A 176 . −15.802 3.541 1.548 1.00 16.14 . 1 1349 ATOM N N LEU A 177 . −15.488 −1.792 0.055 1.00 15.26 . 1 1350 ATOM C CA LEU A 177 . −15.281 −2.884 −0.907 1.00 15.43 . 1 1351 ATOM C C LEU A 177 . −16.261 −4.022 −0.590 1.00 14.16 . 1 1352 ATOM O O LEU A 177 . −16.815 −4.629 −1.529 1.00 14.78 . 1 1353 ATOM C CB LEU A 177 . −13.826 −3.391 −0.848 1.00 18.18 . 1 1354 ATOM C CG LEU A 177 . −12.817 −2.408 −1.448 1.00 21.53 . 1 1355 ATOM C CD1 LEU A 177 . −11.401 −2.922 −1.174 1.00 24.65 . 1 1356 ATOM C CD2 LEU A 177 . −13.041 −2.242 −2.930 1.00 22.33 . 1 1357 ATOM N N ALA A 178 . −16.533 −4.317 0.691 1.00 14.54 . 1 1358 ATOM C CA ALA A 178 . −17.505 −5.362 0.994 1.00 14.94 . 1 1359 ATOM C C ALA A 178 . −18.888 −4.949 0.448 1.00 15.62 . 1 1360 ATOM O O ALA A 178 . −19.619 −5.762 −0.136 1.00 14.81 . 1 1361 ATOM C CB ALA A 178 . −17.565 −5.610 2.476 1.00 14.71 . 1 1362 ATOM N N LEU A 179 . −19.221 −3.665 0.596 1.00 13.28 . 1 1363 ATOM C CA LEU A 179 . −20.487 −3.213 0.064 1.00 13.69 . 1 1364 ATOM C C LEU A 179 . −20.595 −3.313 −1.457 1.00 13.11 . 1 1365 ATOM O O LEU A 179 . −21.576 −3.806 −1.962 1.00 14.44 . 1 1366 ATOM C CB LEU A 179 . −20.736 −1.762 0.475 1.00 12.00 . 1 1367 ATOM C CG LEU A 179 . −21.945 −1.080 −0.191 1.00 13.26 . 1 1368 ATOM C CD1 LEU A 179 . −23.266 −1.681 0.271 1.00 12.61 . 1 1369 ATOM C CD2 LEU A 179 . −21.930 0.402 0.245 1.00 13.30 . 1 1370 ATOM N N ARG A 180 . −19.599 −2.829 −2.191 1.00 12.89 . 1 1371 ATOM C CA ARG A 180 . −19.722 −2.853 −3.658 1.00 13.23 . 1 1372 ATOM C C ARG A 180 . −19.703 −4.279 −4.198 1.00 12.92 . 1 1373 ATOM O O ARG A 180 . −20.180 −4.513 −5.310 1.00 15.00 . 1 1374 ATOM C CB ARG A 180 . −18.643 −1.967 −4.297 1.00 14.89 . 1 1375 ATOM C CG ARG A 180 . −17.218 −2.514 −4.285 1.00 15.84 . 1 1376 ATOM C CD ARG A 180 . −16.935 −3.525 −5.433 1.00 17.07 . 1 1377 ATOM N NE ARG A 180 . −15.542 −3.972 −5.372 1.00 16.89 . 1 1378 ATOM C CZ ARG A 180 . −14.508 −3.345 −5.947 1.00 17.80 . 1 1379 ATOM N NH1 ARG A 180 . −14.686 −2.225 −6.659 1.00 16.23 . 1 1380 ATOM N NH2 ARG A 180 . −13.269 −3.825 −5.768 1.00 18.18 . 1 1381 ATOM N N ASP A 181 . −19.212 −5.225 −3.388 1.00 15.08 . 1 1382 ATOM C CA ASP A 181 . −19.220 −6.656 −3.820 1.00 17.02 . 1 1383 ATOM C C ASP A 181 . −20.589 −7.310 −3.603 1.00 18.57 . 1 1384 ATOM O O ASP A 181 . −20.799 −8.487 −3.958 1.00 19.62 . 1 1385 ATOM C CB ASP A 181 . −18.134 −7.460 −3.080 1.00 18.78 . 1 1386 ATOM C CG ASP A 181 . −16.737 −7.151 −3.593 1.00 19.79 . 1 1387 ATOM O OD1 ASP A 181 . −16.594 −6.574 −4.674 1.00 23.39 . 1 1388 ATOM O OD2 ASP A 181 . −15.755 −7.493 −2.910 1.00 24.94 . 1 1389 ATOM N N CYS A 182 . −21.510 −6.599 −2.970 1.00 17.32 . 1 1390 ATOM C CA CYS A 182 . −22.860 −7.102 −2.749 1.00 18.16 . 1 1391 ATOM C C CYS A 182 . −23.770 −6.796 −3.953 1.00 20.28 . 1 1392 ATOM O O CYS A 182 . −24.473 −5.790 −3.991 1.00 17.40 . 1 1393 ATOM C CB CYS A 182 . −23.488 −6.457 −1.515 1.00 18.49 . 1 1394 ATOM S SG CYS A 182 . −22.798 −6.952 0.059 1.00 19.40 . 1 1395 ATOM N N ASP A 183 . −23.793 −7.681 −4.947 1.00 20.51 . 1 1396 ATOM C CA ASP A 183 . −24.630 −7.404 −6.107 1.00 23.66 . 1 1397 ATOM C C ASP A 183 . −26.081 −7.258 −5.825 1.00 23.27 . 1 1398 ATOM O O ASP A 183 . −26.760 −6.438 −6.453 1.00 25.26 . 1 1399 ATOM C CB ASP A 183 . −24.464 −8.485 −7.154 1.00 27.42 . 1 1400 ATOM C CG ASP A 183 . −23.135 −8.412 −7.824 1.00 30.16 . 1 1401 ATOM O OD1 ASP A 183 . −22.789 −7.303 −8.338 1.00 32.21 . 1 1402 ATOM O OD2 ASP A 183 . −22.440 −9.467 −7.830 1.00 32.75 . 1 1403 ATOM N N PHE A 184 . −26.578 −7.998 −4.855 1.00 21.69 . 1 1404 ATOM C CA PHE A 184 . −27.985 −7.927 −4.528 1.00 22.23 . 1 1405 ATOM C C PHE A 184 . −28.397 −6.524 −4.080 1.00 20.78 . 1 1406 ATOM O O PHE A 184 . −29.580 −6.141 −4.192 1.00 21.83 . 1 1407 ATOM C CB PHE A 184 . −28.344 −8.966 −3.457 1.00 23.64 . 1 1408 ATOM C CG PHE A 184 . −27.698 −8.726 −2.108 1.00 24.77 . 1 1409 ATOM C CD1 PHE A 184 . −28.346 −7.974 −1.135 1.00 25.42 . 1 1410 ATOM C CD2 PHE A 184 . −26.441 −9.285 −1.814 1.00 25.77 . 1 1411 ATOM C CE1 PHE A 184 . −27.756 −7.771 0.128 1.00 26.17 . 1 1412 ATOM C CE2 PHE A 184 . −25.842 −9.090 −0.568 1.00 24.67 . 1 1413 ATOM C CZ PHE A 184 . −26.490 −8.336 0.401 1.00 26.00 . 1 1414 ATOM N N VAL A 185 . −27.439 −5.740 −3.549 1.00 18.88 . 1 1415 ATOM C CA VAL A 185 . −27.799 −4.384 −3.166 1.00 17.31 . 1 1416 ATOM C C VAL A 185 . −27.965 −3.524 −4.414 1.00 16.20 . 1 1417 ATOM O O VAL A 185 . −28.910 −2.709 −4.511 1.00 15.11 . 1 1418 ATOM C CB VAL A 185 . −26.686 −3.746 −2.254 1.00 13.74 . 1 1419 ATOM C CG1 VAL A 185 . −26.910 −2.230 −2.090 1.00 14.81 . 1 1420 ATOM C CG2 VAL A 185 . −26.625 −4.483 −0.931 1.00 16.51 . 1 1421 ATOM N N PHE A 186 . −27.063 −3.687 −5.389 1.00 15.74 . 1 1422 ATOM C CA PHE A 186 . −27.098 −2.793 −6.515 1.00 15.17 . 1 1423 ATOM C C PHE A 186 . −27.854 −3.205 −7.768 1.00 16.91 . 1 1424 ATOM O O PHE A 186 . −28.141 −2.362 −8.611 1.00 16.90 . 1 1425 ATOM C CB PHE A 186 . −25.665 −2.398 −6.879 1.00 14.73 . 1 1426 ATOM C CG PHE A 186 . −24.949 −1.681 −5.738 1.00 12.55 . 1 1427 ATOM C CD1 PHE A 186 . −24.193 −2.384 −4.802 1.00 13.78 . 1 1428 ATOM C CD2 PHE A 186 . −25.137 −0.330 −5.564 1.00 14.30 . 1 1429 ATOM C CE1 PHE A 186 . −23.634 −1.723 −3.692 1.00 12.88 . 1 1430 ATOM C CE2 PHE A 186 . −24.593 0.332 −4.478 1.00 14.22 . 1 1431 ATOM C CZ PHE A 186 . −23.860 −0.312 −3.552 1.00 14.29 . 1 1432 ATOM N N ASP A 187 . −28.199 −4.472 −7.865 1.00 18.08 . 1 1433 ATOM C CA ASP A 187 . −28.945 −4.968 −9.024 1.00 20.10 . 1 1434 ATOM C C ASP A 187 . −30.191 −4.144 −9.340 1.00 18.54 . 1 1435 ATOM O O ASP A 187 . −31.042 −3.882 −8.486 1.00 20.33 . 1 1436 ATOM C CB ASP A 187 . −29.419 −6.417 −8.785 1.00 22.74 . 1 1437 ATOM C CG ASP A 187 . −28.363 −7.455 −8.993 1.00 26.21 . 1 1438 ATOM O OD1 ASP A 187 . −27.273 −7.187 −9.541 1.00 27.23 . 1 1439 ATOM O OD2 ASP A 187 . −28.653 −8.601 −8.589 1.00 29.46 . 1 1440 ATOM N N GLY A 188 . −30.294 −3.712 −10.586 1.00 20.04 . 1 1441 ATOM C CA GLY A 188 . −31.459 −2.971 −10.997 1.00 19.96 . 1 1442 ATOM C C GLY A 188 . −31.523 −1.514 −10.622 1.00 19.50 . 1 1443 ATOM O O GLY A 188 . −32.392 −0.791 −11.136 1.00 21.03 . 1 1444 ATOM N N LEU A 189 . −30.633 −1.030 −9.754 1.00 16.05 . 1 1445 ATOM C CA LEU A 189 . −30.723 0.401 −9.429 1.00 16.86 . 1 1446 ATOM C C LEU A 189 . −30.297 1.304 −10.555 1.00 15.96 . 1 1447 ATOM O O LEU A 189 . −29.354 0.988 −11.303 1.00 16.46 . 1 1448 ATOM C CB LEU A 189 . −29.826 0.768 −8.216 1.00 17.40 . 1 1449 ATOM C CG LEU A 189 . −30.173 0.055 −6.909 1.00 16.35 . 1 1450 ATOM C CD1 LEU A 189 . −29.188 0.527 −5.808 1.00 14.42 . 1 1451 ATOM C CD2 LEU A 189 . −31.640 0.344 −6.490 1.00 17.55 . 1 1452 ATOM N N GLU A 190 . −30.965 2.438 −10.645 1.00 16.35 . 1 1453 ATOM C CA GLU A 190 . −30.545 3.428 −11.590 1.00 16.40 . 1 1454 ATOM C C GLU A 190 . −29.968 4.623 −10.834 1.00 15.17 . 1 1455 ATOM O O GLU A 190 . −29.211 5.399 −11.410 1.00 16.16 . 1 1456 ATOM C CB GLU A 190 . −31.684 3.877 −12.476 1.00 18.41 . 1 1457 ATOM C CG GLU A 190 . −32.119 2.713 −13.377 1.00 23.63 . 1 1458 ATOM C CD GLU A 190 . −33.347 2.988 −14.185 1.00 29.38 . 1 1459 ATOM O OE1 GLU A 190 . −34.122 3.906 −13.829 1.00 31.59 . 1 1460 ATOM O OE2 GLU A 190 . −33.541 2.262 −15.190 1.00 32.39 . 1 1461 ATOM N N SER A 191 . −30.332 4.756 −9.541 1.00 14.62 . 1 1462 ATOM C CA SER A 191 . −29.845 5.882 −8.739 1.00 13.81 . 1 1463 ATOM C C SER A 191 . −29.823 5.462 −7.259 1.00 12.64 . 1 1464 ATOM O O SER A 191 . −30.579 4.609 −6.809 1.00 13.63 . 1 1465 ATOM C CB SER A 191 . −30.759 7.118 −8.891 1.00 14.76 . 1 1466 ATOM O OG SER A 191 . −32.072 6.885 −8.431 1.00 16.01 . 1 1467 ATOM N N ILE A 192 . −28.916 6.095 −6.523 1.00 11.98 . 1 1468 ATOM C CA ILE A 192 . −28.809 5.878 −5.087 1.00 10.55 . 1 1469 ATOM C C ILE A 192 . −28.372 7.182 −4.436 1.00 11.74 . 1 1470 ATOM O O ILE A 192 . −27.615 7.915 −5.034 1.00 13.53 . 1 1471 ATOM C CB ILE A 192 . −27.806 4.778 −4.743 1.00 11.97 . 1 1472 ATOM C CG1 ILE A 192 . −27.859 4.476 −3.255 1.00 12.77 . 1 1473 ATOM C CG2 ILE A 192 . −26.340 5.209 −5.119 1.00 14.50 . 1 1474 ATOM C CD1 ILE A 192 . −27.173 3.149 −2.936 1.00 15.16 . 1 1475 ATOM N N VAL A 193 . −28.873 7.470 −3.248 1.00 10.13 . 1 1476 ATOM C CA VAL A 193 . −28.417 8.619 −2.488 1.00 10.83 . 1 1477 ATOM C C VAL A 193 . −27.770 8.080 −1.186 1.00 10.21 . 1 1478 ATOM O O VAL A 193 . −28.370 7.322 −0.421 1.00 10.38 . 1 1479 ATOM C CB VAL A 193 . −29.611 9.634 −2.195 1.00 10.16 . 1 1480 ATOM C CG1 VAL A 193 . −30.781 8.992 −1.441 1.00 12.58 . 1 1481 ATOM C CG2 VAL A 193 . −29.081 10.811 −1.402 1.00 10.45 . 1 1482 ATOM N N ASP A 194 . −26.534 8.508 −0.953 1.00 10.18 . 1 1483 ATOM C CA ASP A 194 . −25.804 8.115 0.293 1.00 9.44 . 1 1484 ATOM C C ASP A 194 . −26.056 9.218 1.286 1.00 9.67 . 1 1485 ATOM O O ASP A 194 . −25.546 10.319 1.150 1.00 10.84 . 1 1486 ATOM C CB ASP A 194 . −24.330 7.937 −0.017 1.00 10.98 . 1 1487 ATOM C CG ASP A 194 . −23.561 7.399 1.187 1.00 9.35 . 1 1488 ATOM O OD1 ASP A 194 . −24.256 7.138 2.182 1.00 11.05 . 1 1489 ATOM O OD2 ASP A 194 . −22.313 7.233 1.034 1.00 11.48 . 1 1490 ATOM N N VAL A 195 . −26.957 8.925 2.237 1.00 9.85 . 1 1491 ATOM C CA VAL A 195 . −27.412 9.920 3.212 1.00 10.40 . 1 1492 ATOM C C VAL A 195 . −26.413 10.011 4.370 1.00 10.01 . 1 1493 ATOM O O VAL A 195 . −26.171 9.007 5.059 1.00 10.78 . 1 1494 ATOM C CB VAL A 195 . −28.847 9.576 3.682 1.00 8.38 . 1 1495 ATOM C CG1 VAL A 195 . −29.263 10.439 4.850 1.00 11.71 . 1 1496 ATOM C CG2 VAL A 195 . −29.823 9.757 2.487 1.00 10.64 . 1 1497 ATOM N N GLY A 196 . −25.927 11.227 4.622 1.00 10.59 . 1 1498 ATOM C CA GLY A 196 . −24.792 11.375 5.574 1.00 10.68 . 1 1499 ATOM C C GLY A 196 . −23.553 10.779 4.888 1.00 10.99 . 1 1500 ATOM O O GLY A 196 . −22.696 10.191 5.579 1.00 11.17 . 1 1501 ATOM N N GLY A 197 . −23.435 10.936 3.553 1.00 10.76 . 1 1502 ATOM C CA GLY A 197 . −22.341 10.369 2.757 1.00 10.36 . 1 1503 ATOM C C GLY A 197 . −20.951 10.985 2.908 1.00 11.85 . 1 1504 ATOM O O GLY A 197 . −19.977 10.580 2.213 1.00 12.17 . 1 1505 ATOM N N GLY A 198 . −20.862 11.952 3.804 1.00 11.50 . 1 1506 ATOM C CA GLY A 198 . −19.538 12.550 4.021 1.00 13.76 . 1 1507 ATOM C C GLY A 198 . −18.956 13.296 2.820 1.00 12.28 . 1 1508 ATOM O O GLY A 198 . −19.646 14.095 2.140 1.00 13.10 . 1 1509 ATOM N N THR A 199 . −17.683 13.022 2.515 1.00 13.75 . 1 1510 ATOM C CA THR A 199 . −17.040 13.678 1.409 1.00 16.05 . 1 1511 ATOM C C THR A 199 . −17.120 12.793 0.164 1.00 15.18 . 1 1512 ATOM O O THR A 199 . −16.457 13.035 −0.812 1.00 16.46 . 1 1513 ATOM C CB THR A 199 . −15.559 14.013 1.756 1.00 17.67 . 1 1514 ATOM O OG1 THR A 199 . −14.907 12.787 2.129 1.00 19.56 . 1 1515 ATOM C CG2 THR A 199 . −15.497 15.021 2.990 1.00 19.46 . 1 1516 ATOM N N GLY A 200 . −17.931 11.731 0.238 1.00 14.57 . 1 1517 ATOM C CA GLY A 200 . −18.116 10.868 −0.921 1.00 14.56 . 1 1518 ATOM C C GLY A 200 . −17.231 9.651 −1.042 1.00 13.98 . 1 1519 ATOM O O GLY A 200 . −17.175 9.032 −2.105 1.00 14.70 . 1 1520 ATOM N N THR A 201 . −16.600 9.268 0.043 1.00 13.79 . 1 1521 ATOM C CA THR A 201 . −15.708 8.123 −0.005 1.00 15.44 . 1 1522 ATOM C C THR A 201 . −16.383 6.853 −0.502 1.00 14.55 . 1 1523 ATOM O O THR A 201 . −15.884 6.187 −1.438 1.00 14.57 . 1 1524 ATOM C CB THR A 201 . −15.118 7.883 1.331 1.00 15.85 . 1 1525 ATOM O OG1 THR A 201 . −14.500 9.116 1.813 1.00 19.22 . 1 1526 ATOM C CG2 THR A 201 . −14.038 6.767 1.199 1.00 17.30 . 1 1527 ATOM N N THR A 202 . −17.533 6.541 0.110 1.00 13.06 . 1 1528 ATOM C CA THR A 202 . −18.288 5.344 −0.311 1.00 12.69 . 1 1529 ATOM C C THR A 202 . −18.808 5.497 −1.719 1.00 12.44 . 1 1530 ATOM O O THR A 202 . −18.671 4.612 −2.547 1.00 14.16 . 1 1531 ATOM C CB THR A 202 . −19.491 5.145 0.620 1.00 11.22 . 1 1532 ATOM O OG1 THR A 202 . −19.051 4.959 1.964 1.00 12.67 . 1 1533 ATOM C CG2 THR A 202 . −20.321 3.952 0.167 1.00 12.69 . 1 1534 ATOM N N ALA A 203 . −19.394 6.648 −2.044 1.00 12.06 . 1 1535 ATOM C CA ALA A 203 . −19.948 6.855 −3.373 1.00 12.46 . 1 1536 ATOM C C ALA A 203 . −18.926 6.693 −4.480 1.00 13.07 . 1 1537 ATOM O O ALA A 203 . −19.270 6.212 −5.546 1.00 15.11 . 1 1538 ATOM C CB ALA A 203 . −20.570 8.248 −3.440 1.00 12.94 . 1 1539 ATOM N N LYS A 204 . −17.697 7.147 −4.271 1.00 13.95 . 1 1540 ATOM C CA LYS A 204 . −16.688 7.029 −5.309 1.00 15.29 . 1 1541 ATOM C C LYS A 204 . −16.427 5.562 −5.620 1.00 14.39 . 1 1542 ATOM O O LYS A 204 . −16.328 5.185 −6.818 1.00 14.29 . 1 1543 ATOM C CB LYS A 204 . −15.396 7.688 −4.861 1.00 18.18 . 1 1544 ATOM C CG LYS A 204 . −15.522 9.175 −4.790 1.00 22.07 . 1 1545 ATOM C CD LYS A 204 . −14.383 9.721 −3.936 1.00 22.59 . 1 1546 ATOM C CE LYS A 204 . −14.439 11.237 −3.936 1.00 26.81 . 1 1547 ATOM N NZ LYS A 204 . −13.502 11.853 −2.917 1.00 28.77 . 1 1548 ATOM N N ILE A 205 . −16.368 4.726 −4.576 1.00 15.17 . 1 1549 ATOM C CA ILE A 205 . −16.125 3.287 −4.817 1.00 15.96 . 1 1550 ATOM C C ILE A 205 . −17.337 2.676 −5.544 1.00 15.17 . 1 1551 ATOM O O ILE A 205 . −17.198 1.833 −6.454 1.00 15.92 . 1 1552 ATOM C CB ILE A 205 . −15.825 2.588 −3.491 1.00 14.25 . 1 1553 ATOM C CG1 ILE A 205 . −14.441 3.048 −2.996 1.00 19.98 . 1 1554 ATOM C CG2 ILE A 205 . −15.994 1.012 −3.640 1.00 15.44 . 1 1555 ATOM C CD1 ILE A 205 . −14.047 2.520 −1.680 1.00 21.11 . 1 1556 ATOM N N ILE A 206 . −18.534 3.109 −5.154 1.00 14.34 . 1 1557 ATOM C CA ILE A 206 . −19.730 2.644 −5.804 1.00 15.37 . 1 1558 ATOM C C ILE A 206 . −19.693 3.033 −7.277 1.00 15.19 . 1 1559 ATOM O O ILE A 206 . −19.987 2.194 −8.155 1.00 15.54 . 1 1560 ATOM C CB ILE A 206 . −21.043 3.246 −5.139 1.00 14.14 . 1 1561 ATOM C CG1 ILE A 206 . −21.255 2.618 −3.753 1.00 13.23 . 1 1562 ATOM C CG2 ILE A 206 . −22.262 2.998 −6.069 1.00 15.49 . 1 1563 ATOM C CD1 ILE A 206 . −22.407 3.185 −2.980 1.00 13.22 . 1 1564 ATOM N N CYS A 207 . −19.319 4.275 −7.593 1.00 14.68 . 1 1565 ATOM C CA CYS A 207 . −19.327 4.690 −8.990 1.00 16.73 . 1 1566 ATOM C C CYS A 207 . −18.228 4.007 −9.829 1.00 15.73 . 1 1567 ATOM O O CYS A 207 . −18.429 3.773 −11.032 1.00 17.49 . 1 1568 ATOM C CB CYS A 207 . −19.197 6.204 −9.107 1.00 15.49 . 1 1569 ATOM S SG CYS A 207 . −20.694 7.101 −8.548 1.00 21.58 . 1 1570 ATOM N N GLU A 208 . −17.090 3.734 −9.193 1.00 14.81 . 1 1571 ATOM C CA GLU A 208 . −15.977 3.079 −9.895 1.00 15.44 . 1 1572 ATOM C C GLU A 208 . −16.382 1.678 −10.288 1.00 15.62 . 1 1573 ATOM O O GLU A 208 . −15.951 1.152 −11.332 1.00 17.43 . 1 1574 ATOM C CB GLU A 208 . −14.754 3.060 −8.987 1.00 16.36 . 1 1575 ATOM C CG GLU A 208 . −14.153 4.472 −8.976 1.00 16.88 . 1 1576 ATOM C CD GLU A 208 . −13.189 4.713 −7.869 1.00 18.89 . 1 1577 ATOM O OE1 GLU A 208 . −12.953 3.812 −7.055 1.00 20.37 . 1 1578 ATOM O OE2 GLU A 208 . −12.653 5.845 −7.812 1.00 23.67 . 1 1579 ATOM N N THR A 209 . −17.240 1.074 −9.468 1.00 15.19 . 1 1580 ATOM C CA THR A 209 . −17.760 −0.260 −9.655 1.00 14.55 . 1 1581 ATOM C C THR A 209 . −18.933 −0.325 −10.626 1.00 16.02 . 1 1582 ATOM O O THR A 209 . −19.041 −1.243 −11.448 1.00 16.85 . 1 1583 ATOM C CB THR A 209 . −18.232 −0.856 −8.311 1.00 14.19 . 1 1584 ATOM O OG1 THR A 209 . −17.170 −0.744 −7.333 1.00 15.75 . 1 1585 ATOM C CG2 THR A 209 . −18.605 −2.370 −8.439 1.00 15.20 . 1 1586 ATOM N N PHE A 210 . −19.811 0.665 −10.526 1.00 13.88 . 1 1587 ATOM C CA PHE A 210 . −21.033 0.705 −11.357 1.00 15.20 . 1 1588 ATOM C C PHE A 210 . −21.042 2.029 −12.069 1.00 18.06 . 1 1589 ATOM O O PHE A 210 . −21.721 2.964 −11.667 1.00 16.82 . 1 1590 ATOM C CB PHE A 210 . −22.250 0.598 −10.412 1.00 16.06 . 1 1591 ATOM C CG PHE A 210 . −22.221 −0.628 −9.546 1.00 15.77 . 1 1592 ATOM C CD1 PHE A 210 . −21.920 −0.581 −8.178 1.00 16.44 . 1 1593 ATOM C CD2 PHE A 210 . −22.495 −1.859 −10.120 1.00 16.86 . 1 1594 ATOM C CE1 PHE A 210 . −21.898 −1.715 −7.409 1.00 15.65 . 1 1595 ATOM C CE2 PHE A 210 . −22.477 −3.025 −9.364 1.00 16.70 . 1 1596 ATOM C CZ PHE A 210 . −22.177 −2.967 −7.982 1.00 18.05 . 1 1597 ATOM N N PRO A 211 . −20.301 2.123 −13.186 1.00 19.11 . 1 1598 ATOM C CA PRO A 211 . −20.191 3.365 −13.955 1.00 19.87 . 1 1599 ATOM C C PRO A 211 . −21.453 3.972 −14.510 1.00 19.84 . 1 1600 ATOM O O PRO A 211 . −21.447 5.139 −14.862 1.00 21.49 . 1 1601 ATOM C CB PRO A 211 . −19.189 2.996 −15.065 1.00 19.90 . 1 1602 ATOM C CG PRO A 211 . −18.504 1.821 −14.534 1.00 21.00 . 1 1603 ATOM C CD PRO A 211 . −19.580 1.037 −13.835 1.00 21.12 . 1 1604 ATOM N N LYS A 212 . −22.528 3.210 −14.579 1.00 19.05 . 1 1605 ATOM C CA LYS A 212 . −23.740 3.811 −15.118 1.00 18.21 . 1 1606 ATOM C C LYS A 212 . −24.724 4.227 −14.040 1.00 17.23 . 1 1607 ATOM O O LYS A 212 . −25.752 4.777 −14.338 1.00 17.70 . 1 1608 ATOM C CB LYS A 212 . −24.432 2.830 −16.048 1.00 21.63 . 1 1609 ATOM C CG LYS A 212 . −23.554 2.394 −17.223 1.00 25.84 . 1 1610 ATOM C CD LYS A 212 . −24.083 1.092 −17.733 1.00 31.01 . 1 1611 ATOM C CE LYS A 212 . −23.455 0.722 −19.078 1.00 33.76 . 1 1612 ATOM N NZ LYS A 212 . −23.611 −0.745 −19.293 1.00 37.20 . 1 1613 ATOM N N LEU A 213 . −24.395 3.954 −12.790 1.00 15.46 . 1 1614 ATOM C CA LEU A 213 . −25.307 4.277 −11.694 1.00 14.15 . 1 1615 ATOM C C LEU A 213 . −25.198 5.719 −11.261 1.00 15.14 . 1 1616 ATOM O O LEU A 213 . −24.098 6.186 −11.091 1.00 17.47 . 1 1617 ATOM C CB LEU A 213 . −24.938 3.386 −10.501 1.00 13.81 . 1 1618 ATOM C CG LEU A 213 . −25.752 3.515 −9.181 1.00 13.29 . 1 1619 ATOM C CD1 LEU A 213 . −27.227 3.236 −9.451 1.00 14.74 . 1 1620 ATOM C CD2 LEU A 213 . −25.238 2.526 −8.127 1.00 15.26 . 1 1621 ATOM N N LYS A 214 . −26.315 6.406 −11.062 1.00 15.41 . 1 1622 ATOM C CA LYS A 214 . −26.283 7.791 −10.599 1.00 16.89 . 1 1623 ATOM C C LYS A 214 . −26.147 7.741 −9.083 1.00 15.28 . 1 1624 ATOM O O LYS A 214 . −26.908 7.046 −8.412 1.00 15.72 . 1 1625 ATOM C CB LYS A 214 . −27.587 8.506 −10.920 1.00 19.00 . 1 1626 ATOM C CG LYS A 214 . −27.707 9.913 −10.329 1.00 25.66 . 1 1627 ATOM C CD LYS A 214 . −29.130 10.521 −10.439 1.00 29.22 . 1 1628 ATOM C CE LYS A 214 . −29.165 11.901 −9.745 1.00 30.33 . 1 1629 ATOM N NZ LYS A 214 . −30.540 12.525 −9.790 1.00 31.13 . 1 1630 ATOM N N CYS A 215 . −25.208 8.492 −8.516 1.00 15.61 . 1 1631 ATOM C CA CYS A 215 . −25.039 8.470 −7.073 1.00 15.56 . 1 1632 ATOM C C CYS A 215 . −24.997 9.883 −6.571 1.00 12.65 . 1 1633 ATOM O O CYS A 215 . −24.303 10.728 −7.159 1.00 14.40 . 1 1634 ATOM C CB CYS A 215 . −23.730 7.793 −6.730 1.00 17.62 . 1 1635 ATOM S SG CYS A 215 . −23.471 7.554 −4.997 1.00 23.48 . 1 1636 ATOM N N ILE A 216 . −25.804 10.163 −5.561 1.00 11.97 . 1 1637 ATOM C CA ILE A 216 . −25.822 11.500 −4.935 1.00 11.91 . 1 1638 ATOM C C ILE A 216 . −25.202 11.369 −3.546 1.00 11.14 . 1 1639 ATOM O O ILE A 216 . −25.674 10.567 −2.723 1.00 13.24 . 1 1640 ATOM C CB ILE A 216 . −27.283 12.019 −4.760 1.00 12.35 . 1 1641 ATOM C CG1 ILE A 216 . −27.939 12.127 −6.152 1.00 16.17 . 1 1642 ATOM C CG2 ILE A 216 . −27.314 13.330 −3.939 1.00 12.87 . 1 1643 ATOM C CD1 ILE A 216 . −29.465 12.289 −6.030 1.00 18.26 . 1 1644 ATOM N N VAL A 217 . −24.193 12.182 −3.230 1.00 10.49 . 1 1645 ATOM C CA VAL A 217 . −23.596 12.198 −1.887 1.00 11.62 . 1 1646 ATOM C C VAL A 217 . −24.373 13.309 −1.177 1.00 12.01 . 1 1647 ATOM O O VAL A 217 . −24.280 14.464 −1.588 1.00 13.08 . 1 1648 ATOM C CB VAL A 217 . −22.109 12.578 −1.951 1.00 11.30 . 1 1649 ATOM C CG1 VAL A 217 . −21.525 12.730 −0.512 1.00 12.15 . 1 1650 ATOM C CG2 VAL A 217 . −21.337 11.493 −2.747 1.00 11.98 . 1 1651 ATOM N N PHE A 218 . −25.117 12.973 −0.130 1.00 10.54 . 1 1652 ATOM C CA PHE A 218 . −25.937 13.940 0.576 1.00 11.08 . 1 1653 ATOM C C PHE A 218 . −25.424 14.139 1.998 1.00 11.28 . 1 1654 ATOM O O PHE A 218 . −25.294 13.167 2.756 1.00 11.90 . 1 1655 ATOM C CB PHE A 218 . −27.394 13.428 0.597 1.00 10.44 . 1 1656 ATOM C CG PHE A 218 . −28.364 14.312 1.326 1.00 11.15 . 1 1657 ATOM C CD1 PHE A 218 . −28.838 15.447 0.746 1.00 11.52 . 1 1658 ATOM C CD2 PHE A 218 . −28.798 13.976 2.590 1.00 11.23 . 1 1659 ATOM C CE1 PHE A 218 . −29.762 16.275 1.426 1.00 12.98 . 1 1660 ATOM C CE2 PHE A 218 . −29.715 14.763 3.288 1.00 13.04 . 1 1661 ATOM C CZ PHE A 218 . −30.204 15.931 2.691 1.00 12.82 . 1 1662 ATOM N N ASP A 219 . −25.081 15.366 2.374 1.00 10.98 . 1 1663 ATOM C CA ASP A 219 . −24.600 15.576 3.734 1.00 10.94 . 1 1664 ATOM C C ASP A 219 . −24.874 17.083 4.029 1.00 10.21 . 1 1665 ATOM O O ASP A 219 . −25.529 17.773 3.237 1.00 10.68 . 1 1666 ATOM C CB ASP A 219 . −23.092 15.208 3.874 1.00 11.12 . 1 1667 ATOM C CG ASP A 219 . −22.717 14.783 5.307 1.00 11.27 . 1 1668 ATOM O OD1 ASP A 219 . −22.799 15.687 6.195 1.00 13.47 . 1 1669 ATOM O OD2 ASP A 219 . −22.402 13.590 5.543 1.00 11.53 . 1 1670 ATOM N N ARG A 220 . −24.422 17.532 5.198 1.00 11.69 . 1 1671 ATOM C CA ARG A 220 . −24.650 18.923 5.612 1.00 12.10 . 1 1672 ATOM C C ARG A 220 . −23.904 19.841 4.662 1.00 12.50 . 1 1673 ATOM O O ARG A 220 . −22.856 19.522 4.126 1.00 12.66 . 1 1674 ATOM C CB ARG A 220 . −24.192 19.090 7.052 1.00 11.78 . 1 1675 ATOM C CG ARG A 220 . −24.943 18.148 8.005 1.00 14.23 . 1 1676 ATOM C CD ARG A 220 . −24.487 18.334 9.463 1.00 16.60 . 1 1677 ATOM N NE ARG A 220 . −23.051 18.213 9.655 1.00 20.74 . 1 1678 ATOM C CZ ARG A 220 . −22.233 19.259 9.871 1.00 22.11 . 1 1679 ATOM N NH1 ARG A 220 . −22.730 20.504 9.921 1.00 22.86 . 1 1680 ATOM N NH2 ARG A 220 . −20.936 19.062 10.040 1.00 20.93 . 1 1681 ATOM N N PRO A 221 . −24.448 21.056 4.459 1.00 12.48 . 1 1682 ATOM C CA PRO A 221 . −23.807 21.986 3.537 1.00 13.49 . 1 1683 ATOM C C PRO A 221 . −22.335 22.245 3.781 1.00 14.19 . 1 1684 ATOM O O PRO A 221 . −21.551 22.311 2.836 1.00 15.84 . 1 1685 ATOM C CB PRO A 221 . −24.666 23.245 3.672 1.00 14.15 . 1 1686 ATOM C CG PRO A 221 . −26.043 22.666 3.919 1.00 13.62 . 1 1687 ATOM C CD PRO A 221 . −25.751 21.543 4.922 1.00 13.79 . 1 1688 ATOM N N GLN A 222 . −21.933 22.379 5.044 1.00 16.13 . 1 1689 ATOM C CA GLN A 222 . −20.507 22.637 5.272 1.00 18.16 . 1 1690 ATOM C C GLN A 222 . −19.599 21.480 4.912 1.00 19.59 . 1 1691 ATOM O O GLN A 222 . −18.415 21.665 4.615 1.00 22.00 . 1 1692 ATOM C CB GLN A 222 . −20.215 23.046 6.717 1.00 22.02 . 1 1693 ATOM C CG GLN A 222 . −18.710 23.424 6.778 1.00 26.15 . 1 1694 ATOM C CD GLN A 222 . −18.305 24.316 7.956 1.00 28.60 . 1 1695 ATOM O OE1 GLN A 222 . −17.134 24.304 8.360 1.00 29.48 . 1 1696 ATOM N NE2 GLN A 222 . −19.263 25.077 8.511 1.00 30.00 . 1 1697 ATOM N N VAL A 223 . −20.138 20.272 4.941 1.00 15.38 . 1 1698 ATOM C CA VAL A 223 . −19.356 19.112 4.619 1.00 15.91 . 1 1699 ATOM C C VAL A 223 . −19.147 19.006 3.099 1.00 16.50 . 1 1700 ATOM O O VAL A 223 . −18.048 18.693 2.631 1.00 18.45 . 1 1701 ATOM C CB VAL A 223 . −20.072 17.822 5.145 1.00 15.33 . 1 1702 ATOM C CG1 VAL A 223 . −19.339 16.579 4.594 1.00 15.90 . 1 1703 ATOM C CG2 VAL A 223 . −20.046 17.822 6.692 1.00 14.90 . 1 1704 ATOM N N VAL A 224 . −20.179 19.292 2.317 1.00 16.86 . 1 1705 ATOM C CA VAL A 224 . −19.999 19.075 0.876 1.00 19.12 . 1 1706 ATOM C C VAL A 224 . −19.699 20.320 0.077 1.00 22.69 . 1 1707 ATOM O O VAL A 224 . −19.552 20.251 −1.147 1.00 22.44 . 1 1708 ATOM C CB VAL A 224 . −21.227 18.319 0.249 1.00 18.73 . 1 1709 ATOM C CG1 VAL A 224 . −21.391 16.965 0.884 1.00 20.01 . 1 1710 ATOM C CG2 VAL A 224 . −22.450 19.156 0.388 1.00 19.49 . 1 1711 ATOM N N GLU A 225 . −19.548 21.450 0.773 1.00 26.66 . 1 1712 ATOM C CA GLU A 225 . −19.246 22.693 0.065 1.00 30.72 . 1 1713 ATOM C C GLU A 225 . −17.907 22.598 −0.639 1.00 31.02 . 1 1714 ATOM O O GLU A 225 . −16.922 22.014 −0.149 1.00 32.83 . 1 1715 ATOM C CB GLU A 225 . −19.305 23.931 0.989 1.00 32.14 . 1 1716 ATOM C CG GLU A 225 . −18.235 24.050 2.052 1.00 35.50 . 1 1717 ATOM C CD GLU A 225 . −18.313 25.422 2.765 1.00 36.90 . 1 1718 ATOM O OE1 GLU A 225 . −19.391 25.758 3.304 1.00 37.94 . 1 1719 ATOM O OE2 GLU A 225 . −17.309 26.173 2.772 1.00 39.64 . 1 1720 ATOM N N ASN A 226 . −17.895 23.129 −1.839 1.00 32.97 . 1 1721 ATOM C CA ASN A 226 . −16.690 23.126 −2.638 1.00 32.75 . 1 1722 ATOM C C ASN A 226 . −16.250 21.751 −3.091 1.00 32.23 . 1 1723 ATOM O O ASN A 226 . −15.119 21.633 −3.580 1.00 32.13 . 1 1724 ATOM C CB ASN A 226 . −15.504 23.748 −1.882 1.00 35.28 . 1 1725 ATOM C CG ASN A 226 . −15.833 25.080 −1.268 1.00 36.98 . 1 1726 ATOM O OD1 ASN A 226 . −16.239 26.015 −1.957 1.00 37.76 . 1 1727 ATOM N ND2 ASN A 226 . −15.655 25.178 0.045 1.00 37.81 . 1 1728 ATOM N N LEU A 227 . −17.067 20.709 −2.886 1.00 29.20 . 1 1729 ATOM C CA LEU A 227 . −16.664 19.406 −3.395 1.00 29.38 . 1 1730 ATOM C C LEU A 227 . −17.192 19.316 −4.806 1.00 29.38 . 1 1731 ATOM O O LEU A 227 . −18.277 19.805 −5.096 1.00 30.45 . 1 1732 ATOM C CB LEU A 227 . −17.222 18.246 −2.559 1.00 27.68 . 1 1733 ATOM C CG LEU A 227 . −16.638 18.092 −1.153 1.00 26.29 . 1 1734 ATOM C CD1 LEU A 227 . −17.205 16.836 −0.550 1.00 26.24 . 1 1735 ATOM C CD2 LEU A 227 . −15.114 18.012 −1.182 1.00 26.90 . 1 1736 ATOM N N SER A 228 . −16.412 18.722 −5.696 1.00 31.48 . 1 1737 ATOM C CA SER A 228 . −16.846 18.593 −7.086 1.00 32.35 . 1 1738 ATOM C C SER A 228 . −17.046 17.145 −7.464 1.00 31.25 . 1 1739 ATOM O O SER A 228 . −16.207 16.292 −7.164 1.00 31.29 . 1 1740 ATOM C CB SER A 228 . −15.822 19.221 −8.035 1.00 33.35 . 1 1741 ATOM O OG SER A 228 . −15.930 20.631 −8.003 1.00 37.40 . 1 1742 ATOM N N GLY A 229 . −18.145 16.870 −8.145 1.00 31.55 . 1 1743 ATOM C CA GLY A 229 . −18.388 15.496 −8.525 1.00 32.42 . 1 1744 ATOM C C GLY A 229 . −17.908 15.260 −9.939 1.00 33.01 . 1 1745 ATOM O O GLY A 229 . −17.034 15.976 −10.448 1.00 34.21 . 1 1746 ATOM N N SER A 230 . −18.452 14.244 −10.585 1.00 33.09 . 1 1747 ATOM C CA SER A 230 . −18.073 13.966 −11.952 1.00 34.29 . 1 1748 ATOM C C SER A 230 . −18.833 12.772 −12.478 1.00 34.11 . 1 1749 ATOM O O SER A 230 . −19.066 11.784 −11.747 1.00 33.37 . 1 1750 ATOM C CB SER A 230 . −16.554 13.738 −12.060 1.00 35.40 . 1 1751 ATOM O OG SER A 230 . −16.080 12.847 −11.060 1.00 38.93 . 1 1752 ATOM N N ASN A 231 . −19.231 12.867 −13.743 1.00 33.45 . 1 1753 ATOM C CA ASN A 231 . −19.963 11.804 −14.395 1.00 32.77 . 1 1754 ATOM C C ASN A 231 . −20.714 10.904 −13.418 1.00 30.85 . 1 1755 ATOM O O ASN A 231 . −20.152 10.015 −12.769 1.00 33.99 . 1 1756 ATOM C CB ASN A 231 . −19.021 10.973 −15.271 1.00 35.83 . 1 1757 ATOM C CG ASN A 231 . −19.728 9.798 −15.970 1.00 37.81 . 1 1758 ATOM O OD1 ASN A 231 . −20.773 9.969 −16.649 1.00 39.13 . 1 1759 ATOM N ND2 ASN A 231 . −19.159 8.584 −15.799 1.00 38.15 . 1 1760 ATOM N N ASN A 232 . −21.990 11.167 −13.315 1.00 27.86 . 1 1761 ATOM C CA ASN A 232 . −22.872 10.393 −12.463 1.00 21.36 . 1 1762 ATOM C C ASN A 232 . −22.776 10.575 −10.956 1.00 19.27 . 1 1763 ATOM O O ASN A 232 . −23.727 10.193 −10.280 1.00 20.10 . 1 1764 ATOM C CB ASN A 232 . −22.800 8.905 −12.814 1.00 23.03 . 1 1765 ATOM C CG ASN A 232 . −23.312 8.627 −14.216 1.00 24.07 . 1 1766 ATOM O OD1 ASN A 232 . −24.062 9.430 −14.800 1.00 24.74 . 1 1767 ATOM N ND2 ASN A 232 . −22.896 7.490 −14.772 1.00 26.35 . 1 1768 ATOM N N LEU A 233 . −21.683 11.168 −10.435 1.00 17.10 . 1 1769 ATOM C CA LEU A 233 . −21.541 11.426 −8.998 1.00 17.19 . 1 1770 ATOM C C LEU A 233 . −21.744 12.922 −8.739 1.00 16.30 . 1 1771 ATOM O O LEU A 233 . −21.059 13.769 −9.341 1.00 18.99 . 1 1772 ATOM C CB LEU A 233 . −20.163 10.973 −8.454 1.00 16.90 . 1 1773 ATOM C CG LEU A 233 . −20.060 10.944 −6.908 1.00 20.30 . 1 1774 ATOM C CD1 LEU A 233 . −18.934 10.050 −6.422 1.00 22.96 . 1 1775 ATOM C CD2 LEU A 233 . −19.822 12.326 −6.457 1.00 21.45 . 1 1776 ATOM N N THR A 234 . −22.725 13.271 −7.915 1.00 14.87 . 1 1777 ATOM C CA THR A 234 . −22.986 14.664 −7.566 1.00 15.06 . 1 1778 ATOM C C THR A 234 . −23.079 14.816 −6.066 1.00 14.89 . 1 1779 ATOM O O THR A 234 . −23.193 13.810 −5.373 1.00 14.79 . 1 1780 ATOM C CB THR A 234 . −24.287 15.174 −8.162 1.00 16.81 . 1 1781 ATOM O OG1 THR A 234 . −25.380 14.307 −7.804 1.00 16.83 . 1 1782 ATOM C CG2 THR A 234 . −24.161 15.249 −9.691 1.00 19.32 . 1 1783 ATOM N N TYR A 235 . −22.963 16.041 −5.576 1.00 13.56 . 1 1784 ATOM C CA TYR A 235 . −23.047 16.323 −4.147 1.00 13.03 . 1 1785 ATOM C C TYR A 235 . −24.231 17.233 −3.917 1.00 13.48 . 1 1786 ATOM O O TYR A 235 . −24.456 18.191 −4.689 1.00 15.76 . 1 1787 ATOM C CB TYR A 235 . −21.786 17.061 −3.652 1.00 13.17 . 1 1788 ATOM C CG TYR A 235 . −20.550 16.191 −3.691 1.00 15.69 . 1 1789 ATOM C CD1 TYR A 235 . −19.769 16.112 −4.841 1.00 17.08 . 1 1790 ATOM C CD2 TYR A 235 . −20.180 15.447 −2.571 1.00 16.44 . 1 1791 ATOM C CE1 TYR A 235 . −18.670 15.312 −4.874 1.00 17.56 . 1 1792 ATOM C CE2 TYR A 235 . −19.071 14.643 −2.580 1.00 17.91 . 1 1793 ATOM C CZ TYR A 235 . −18.322 14.569 −3.727 1.00 18.51 . 1 1794 ATOM O OH TYR A 235 . −17.233 13.677 −3.758 1.00 23.36 . 1 1795 ATOM N N VAL A 236 . −24.992 16.958 −2.865 1.00 12.15 . 1 1796 ATOM C CA VAL A 236 . −26.128 17.789 −2.462 1.00 12.28 . 1 1797 ATOM C C VAL A 236 . −26.009 18.099 −0.971 1.00 12.76 . 1 1798 ATOM O O VAL A 236 . −25.839 17.225 −0.132 1.00 13.05 . 1 1799 ATOM C CB VAL A 236 . −27.454 17.078 −2.700 1.00 11.27 . 1 1800 ATOM C CG1 VAL A 236 . −28.606 17.905 −2.099 1.00 10.33 . 1 1801 ATOM C CG2 VAL A 236 . −27.718 16.960 −4.209 1.00 13.63 . 1 1802 ATOM N N GLY A 237 . −26.058 19.400 −0.659 1.00 11.47 . 1 1803 ATOM C CA GLY A 237 . −26.012 19.840 0.742 1.00 13.45 . 1 1804 ATOM C C GLY A 237 . −27.419 19.975 1.304 1.00 13.40 . 1 1805 ATOM O O GLY A 237 . −28.267 20.582 0.666 1.00 16.77 . 1 1806 ATOM N N GLY A 238 . −27.688 19.408 2.477 1.00 12.05 . 1 1807 ATOM C CA GLY A 238 . −29.030 19.508 3.031 1.00 12.94 . 1 1808 ATOM C C GLY A 238 . −29.125 19.041 4.460 1.00 11.40 . 1 1809 ATOM O O GLY A 238 . −28.082 18.999 5.172 1.00 13.17 . 1 1810 ATOM N N ASP A 239 . −30.337 18.694 4.883 1.00 12.43 . 1 1811 ATOM C CA ASP A 239 . −30.608 18.241 6.249 1.00 11.71 . 1 1812 ATOM C C ASP A 239 . −31.505 17.008 6.098 1.00 11.17 . 1 1813 ATOM O O ASP A 239 . −32.636 17.104 5.621 1.00 12.61 . 1 1814 ATOM C CB ASP A 239 . −31.344 19.363 7.022 1.00 14.01 . 1 1815 ATOM C CG ASP A 239 . −31.791 18.918 8.385 1.00 16.41 . 1 1816 ATOM O OD1 ASP A 239 . −31.422 17.837 8.894 1.00 12.95 . 1 1817 ATOM O OD2 ASP A 239 . −32.606 19.685 8.964 1.00 22.93 . 1 1818 ATOM N N MET A 240 . −31.009 15.850 6.560 1.00 11.62 . 1 1819 ATOM C CA MET A 240 . −31.770 14.641 6.432 1.00 10.90 . 1 1820 ATOM C C MET A 240 . −33.036 14.631 7.257 1.00 12.43 . 1 1821 ATOM O O MET A 240 . −33.918 13.807 7.004 1.00 11.74 . 1 1822 ATOM C CB MET A 240 . −30.892 13.437 6.795 1.00 11.77 . 1 1823 ATOM C CG MET A 240 . −30.465 13.390 8.249 1.00 10.98 . 1 1824 ATOM S SD MET A 240 . −29.271 12.024 8.470 1.00 13.65 . 1 1825 ATOM C CE MET A 240 . −28.810 12.274 10.220 1.00 13.20 . 1 1826 ATOM N N PHE A 241 . −33.172 15.549 8.218 1.00 12.52 . 1 1827 ATOM C CA PHE A 241 . −34.386 15.590 9.025 1.00 13.12 . 1 1828 ATOM C C PHE A 241 . −35.481 16.397 8.327 1.00 12.75 . 1 1829 ATOM O O PHE A 241 . −36.605 16.364 8.797 1.00 13.79 . 1 1830 ATOM C CB PHE A 241 . −34.095 16.231 10.384 1.00 14.10 . 1 1831 ATOM C CG PHE A 241 . −33.256 15.359 11.296 1.00 11.65 . 1 1832 ATOM C CD1 PHE A 241 . −31.884 15.405 11.276 1.00 11.65 . 1 1833 ATOM C CD2 PHE A 241 . −33.891 14.435 12.134 1.00 13.21 . 1 1834 ATOM C CE1 PHE A 241 . −31.119 14.510 12.126 1.00 12.63 . 1 1835 ATOM C CE2 PHE A 241 . −33.137 13.557 12.945 1.00 13.36 . 1 1836 ATOM C CZ PHE A 241 . −31.778 13.603 12.941 1.00 13.03 . 1 1837 ATOM N N THR A 242 . −35.121 17.082 7.245 1.00 12.41 . 1 1838 ATOM C CA THR A 242 . −36.035 17.955 6.499 1.00 14.31 . 1 1839 ATOM C C THR A 242 . −36.404 17.456 5.118 1.00 12.91 . 1 1840 ATOM O O THR A 242 . −37.560 17.423 4.788 1.00 13.39 . 1 1841 ATOM C CB THR A 242 . −35.427 19.368 6.429 1.00 16.62 . 1 1842 ATOM O OG1 THR A 242 . −35.200 19.863 7.754 1.00 19.86 . 1 1843 ATOM C CG2 THR A 242 . −36.391 20.292 5.763 1.00 20.79 . 1 1844 ATOM N N SER A 243 . −35.428 17.018 4.320 1.00 12.57 . 1 1845 ATOM C CA SER A 243 . −35.724 16.529 2.983 1.00 11.93 . 1 1846 ATOM C C SER A 243 . −34.520 15.824 2.407 1.00 12.95 . 1 1847 ATOM O O SER A 243 . −33.417 16.375 2.423 1.00 12.45 . 1 1848 ATOM C CB SER A 243 . −36.069 17.706 2.072 1.00 14.79 . 1 1849 ATOM O OG SER A 243 . −36.228 17.247 0.715 1.00 15.59 . 1 1850 ATOM N N ILE A 244 . −34.745 14.586 1.947 1.00 11.11 . 1 1851 ATOM C CA ILE A 244 . −33.680 13.806 1.330 1.00 11.74 . 1 1852 ATOM C C ILE A 244 . −34.022 13.664 −0.161 1.00 11.52 . 1 1853 ATOM O O ILE A 244 . −35.173 13.357 −0.501 1.00 11.77 . 1 1854 ATOM C CB ILE A 244 . −33.621 12.393 1.937 1.00 9.89 . 1 1855 ATOM C CG1 ILE A 244 . −33.182 12.501 3.444 1.00 11.12 . 1 1856 ATOM C CG2 ILE A 244 . −32.683 11.495 1.078 1.00 12.00 . 1 1857 ATOM C CD1 ILE A 244 . −33.258 11.193 4.226 1.00 12.72 . 1 1858 ATOM N N PRO A 245 . −33.060 13.898 −1.072 1.00 12.16 . 1 1859 ATOM C CA PRO A 245 . −33.368 13.757 −2.508 1.00 11.97 . 1 1860 ATOM C C PRO A 245 . −33.941 12.401 −2.919 1.00 12.93 . 1 1861 ATOM O O PRO A 245 . −33.507 11.355 −2.404 1.00 12.41 . 1 1862 ATOM C CB PRO A 245 . −32.014 13.950 −3.188 1.00 12.94 . 1 1863 ATOM C CG PRO A 245 . −31.260 14.789 −2.177 1.00 12.37 . 1 1864 ATOM C CD PRO A 245 . −31.657 14.286 −0.850 1.00 13.05 . 1 1865 ATOM N N ASN A 246 . −34.913 12.431 −3.839 1.00 13.27 . 1 1866 ATOM C CA ASN A 246 . −35.439 11.170 −4.372 1.00 11.98 . 1 1867 ATOM C C ASN A 246 . −34.352 10.349 −5.056 1.00 11.59 . 1 1868 ATOM O O ASN A 246 . −33.436 10.854 −5.705 1.00 12.05 . 1 1869 ATOM C CB ASN A 246 . −36.505 11.421 −5.486 1.00 15.37 . 1 1870 ATOM C CG ASN A 246 . −37.714 12.196 −4.996 1.00 16.48 . 1 1871 ATOM O OD1 ASN A 246 . −38.337 12.886 −5.790 1.00 22.04 . 1 1872 ATOM N ND2 ASN A 246 . −38.068 12.070 −3.751 1.00 16.06 . 1 1873 ATOM N N ALA A 247 . −34.449 9.036 −4.864 1.00 12.40 . 1 1874 ATOM C CA ALA A 247 . −33.547 8.111 −5.577 1.00 11.92 . 1 1875 ATOM C C ALA A 247 . −34.195 6.717 −5.481 1.00 10.99 . 1 1876 ATOM O O ALA A 247 . −35.153 6.512 −4.725 1.00 13.30 . 1 1877 ATOM C CB ALA A 247 . −32.109 8.051 −4.939 1.00 12.19 . 1 1878 ATOM N N ASP A 248 . −33.645 5.730 −6.213 1.00 12.52 . 1 1879 ATOM C CA ASP A 248 . −34.210 4.386 −6.164 1.00 12.72 . 1 1880 ATOM C C ASP A 248 . −33.872 3.708 −4.810 1.00 12.16 . 1 1881 ATOM O O ASP A 248 . −34.520 2.770 −4.388 1.00 13.09 . 1 1882 ATOM C CB ASP A 248 . −33.651 3.475 −7.267 1.00 11.97 . 1 1883 ATOM C CG ASP A 248 . −34.101 3.842 −8.667 1.00 15.99 . 1 1884 ATOM O OD1 ASP A 248 . −35.205 4.408 −8.810 1.00 17.80 . 1 1885 ATOM O OD2 ASP A 248 . −33.330 3.491 −9.601 1.00 18.81 . 1 1886 ATOM N N ALA A 249 . −32.819 4.187 −4.132 1.00 11.29 . 1 1887 ATOM C CA ALA A 249 . −32.411 3.616 −2.882 1.00 11.95 . 1 1888 ATOM C C ALA A 249 . −31.661 4.658 −2.082 1.00 10.15 . 1 1889 ATOM O O ALA A 249 . −31.108 5.612 −2.646 1.00 10.20 . 1 1890 ATOM C CB ALA A 249 . −31.455 2.419 −3.125 1.00 11.72 . 1 1891 ATOM N N VAL A 250 . −31.678 4.453 −0.767 1.00 10.76 . 1 1892 ATOM C CA VAL A 250 . −30.911 5.307 0.170 1.00 10.68 . 1 1893 ATOM C C VAL A 250 . −29.922 4.429 0.876 1.00 11.97 . 1 1894 ATOM O O VAL A 250 . −30.247 3.300 1.222 1.00 12.58 . 1 1895 ATOM C CB VAL A 250 . −31.838 5.914 1.258 1.00 11.80 . 1 1896 ATOM C CG1 VAL A 250 . −31.061 6.467 2.468 1.00 12.26 . 1 1897 ATOM C CG2 VAL A 250 . −32.641 7.089 0.641 1.00 13.02 . 1 1898 ATOM N N LEU A 251 . −28.697 4.901 1.029 1.00 9.09 . 1 1899 ATOM C CA LEU A 251 . −27.669 4.211 1.836 1.00 10.58 . 1 1900 ATOM C C LEU A 251 . −27.473 4.997 3.149 1.00 9.14 . 1 1901 ATOM O O LEU A 251 . −27.374 6.209 3.123 1.00 10.83 . 1 1902 ATOM C CB LEU A 251 . −26.308 4.127 1.089 1.00 10.04 . 1 1903 ATOM C CG LEU A 251 . −25.160 3.425 1.900 1.00 11.27 . 1 1904 ATOM C CD1 LEU A 251 . −25.443 1.975 2.096 1.00 14.05 . 1 1905 ATOM C CD2 LEU A 251 . −23.843 3.628 1.203 1.00 13.81 . 1 1906 ATOM N N LEU A 252 . −27.423 4.284 4.273 1.00 9.90 . 1 1907 ATOM C CA LEU A 252 . −27.149 4.902 5.595 1.00 10.13 . 1 1908 ATOM C C LEU A 252 . −25.962 4.109 6.201 1.00 8.85 . 1 1909 ATOM O O LEU A 252 . −26.209 3.033 6.796 1.00 9.75 . 1 1910 ATOM C CB LEU A 252 . −28.331 4.732 6.532 1.00 9.87 . 1 1911 ATOM C CG LEU A 252 . −29.552 5.601 6.093 1.00 9.77 . 1 1912 ATOM C CD1 LEU A 252 . −30.827 5.069 6.870 1.00 9.25 . 1 1913 ATOM C CD2 LEU A 252 . −29.306 7.104 6.340 1.00 11.68 . 1 1914 ATOM N N LYS A 253 . −24.733 4.590 6.010 1.00 9.79 . 1 1915 ATOM C CA LYS A 253 . −23.546 3.887 6.551 1.00 10.03 . 1 1916 ATOM C C LYS A 253 . −23.089 4.620 7.798 1.00 11.40 . 1 1917 ATOM O O LYS A 253 . −22.744 5.791 7.765 1.00 11.41 . 1 1918 ATOM C CB LYS A 253 . −22.442 3.813 5.495 1.00 11.17 . 1 1919 ATOM C CG LYS A 253 . −21.055 3.289 6.030 1.00 11.47 . 1 1920 ATOM C CD LYS A 253 . −20.030 3.207 4.944 1.00 11.63 . 1 1921 ATOM C CE LYS A 253 . −18.635 2.816 5.519 1.00 13.61 . 1 1922 ATOM N NZ LYS A 253 . −17.919 4.112 5.702 1.00 14.20 . 1 1923 ATOM N N TYR A 254 . −23.100 3.900 8.919 1.00 11.10 . 1 1924 ATOM C CA TYR A 254 . −22.682 4.496 10.217 1.00 13.17 . 1 1925 ATOM C C TYR A 254 . −23.487 5.768 10.556 1.00 14.06 . 1 1926 ATOM O O TYR A 254 . −22.927 6.742 11.129 1.00 13.23 . 1 1927 ATOM C CB TYR A 254 . −21.205 4.849 10.148 1.00 13.59 . 1 1928 ATOM C CG TYR A 254 . −20.231 3.727 10.345 1.00 11.52 . 1 1929 ATOM C CD1 TYR A 254 . −19.075 3.705 9.601 1.00 13.28 . 1 1930 ATOM C CD2 TYR A 254 . −20.390 2.806 11.381 1.00 13.71 . 1 1931 ATOM C CE1 TYR A 254 . −18.040 2.804 9.876 1.00 12.98 . 1 1932 ATOM C CE2 TYR A 254 . −19.351 1.874 11.664 1.00 14.33 . 1 1933 ATOM C CZ TYR A 254 . −18.204 1.899 10.923 1.00 13.44 . 1 1934 ATOM O OH TYR A 254 . −17.203 1.024 11.257 1.00 15.78 . 1 1935 ATOM N N ILE A 255 . −24.780 5.799 10.211 1.00 11.12 . 1 1936 ATOM C CA ILE A 255 . −25.647 6.960 10.542 1.00 10.23 . 1 1937 ATOM C C ILE A 255 . −26.552 6.655 11.742 1.00 11.61 . 1 1938 ATOM O O ILE A 255 . −26.508 7.308 12.774 1.00 12.20 . 1 1939 ATOM C CB ILE A 255 . −26.588 7.313 9.313 1.00 10.16 . 1 1940 ATOM C CG1 ILE A 255 . −25.726 7.560 8.076 1.00 11.50 . 1 1941 ATOM C CG2 ILE A 255 . −27.461 8.495 9.648 1.00 12.03 . 1 1942 ATOM C CD1 ILE A 255 . −24.672 8.705 8.220 1.00 9.85 . 1 1943 ATOM N N LEU A 256 . −27.418 5.648 11.622 1.00 10.58 . 1 1944 ATOM C CA LEU A 256 . −28.412 5.384 12.656 1.00 9.78 . 1 1945 ATOM C C LEU A 256 . −27.893 5.091 14.052 1.00 10.27 . 1 1946 ATOM O O LEU A 256 . −28.527 5.437 15.046 1.00 11.98 . 1 1947 ATOM C CB LEU A 256 . −29.422 4.309 12.176 1.00 12.67 . 1 1948 ATOM C CG LEU A 256 . −30.135 4.717 10.878 1.00 11.72 . 1 1949 ATOM C CD1 LEU A 256 . −31.070 3.522 10.507 1.00 12.84 . 1 1950 ATOM C CD2 LEU A 256 . −30.942 6.047 11.044 1.00 13.49 . 1 1951 ATOM N N HIS A 257 . −26.706 4.536 14.144 1.00 10.87 . 1 1952 ATOM C CA HIS A 257 . −26.221 4.258 15.508 1.00 12.33 . 1 1953 ATOM C C HIS A 257 . −25.824 5.541 16.239 1.00 13.92 . 1 1954 ATOM O O HIS A 257 . −25.501 5.480 17.448 1.00 13.14 . 1 1955 ATOM C CB HIS A 257 . −25.033 3.285 15.469 1.00 12.68 . 1 1956 ATOM C CG HIS A 257 . −23.743 3.884 15.022 1.00 13.36 . 1 1957 ATOM N ND1 HIS A 257 . −22.522 3.473 15.549 1.00 12.65 . 1 1958 ATOM C CD2 HIS A 257 . −23.449 4.838 14.097 1.00 13.36 . 1 1959 ATOM C CE1 HIS A 257 . −21.551 4.144 14.952 1.00 15.42 . 1 1960 ATOM N NE2 HIS A 257 . −22.082 4.977 14.067 1.00 14.93 . 1 1961 ATOM N N ASN A 258 . −25.824 6.687 15.550 1.00 12.69 . 1 1962 ATOM C CA ASN A 258 . −25.464 7.970 16.175 1.00 14.04 . 1 1963 ATOM C C ASN A 258 . −26.706 8.699 16.699 1.00 11.34 . 1 1964 ATOM O O ASN A 258 . −26.581 9.927 17.068 1.00 13.21 . 1 1965 ATOM C CB ASN A 258 . −24.832 8.978 15.162 1.00 15.71 . 1 1966 ATOM C CG ASN A 258 . −23.555 8.521 14.532 1.00 20.32 . 1 1967 ATOM O OD1 ASN A 258 . −23.385 8.703 13.310 1.00 25.73 . 1 1968 ATOM N ND2 ASN A 258 . −22.655 8.022 15.293 1.00 19.14 . 1 1969 ATOM N N TRP A 259 . −27.892 8.070 16.733 1.00 12.23 . 1 1970 ATOM C CA TRP A 259 . −29.119 8.786 17.111 1.00 11.42 . 1 1971 ATOM C C TRP A 259 . −30.038 7.974 17.997 1.00 12.06 . 1 1972 ATOM O O TRP A 259 . −30.046 6.722 17.938 1.00 11.79 . 1 1973 ATOM C CB TRP A 259 . −29.906 9.177 15.801 1.00 13.46 . 1 1974 ATOM C CG TRP A 259 . −29.119 9.968 14.858 1.00 14.08 . 1 1975 ATOM C CD1 TRP A 259 . −28.345 9.490 13.828 1.00 14.35 . 1 1976 ATOM C CD2 TRP A 259 . −28.968 11.388 14.854 1.00 13.37 . 1 1977 ATOM N NE1 TRP A 259 . −27.715 10.523 13.195 1.00 14.60 . 1 1978 ATOM C CE2 TRP A 259 . −28.078 11.701 13.804 1.00 13.75 . 1 1979 ATOM C CE3 TRP A 259 . −29.494 12.422 15.638 1.00 14.78 . 1 1980 ATOM C CZ2 TRP A 259 . −27.686 13.007 13.505 1.00 14.35 . 1 1981 ATOM C CZ3 TRP A 259 . −29.115 13.738 15.345 1.00 17.07 . 1 1982 ATOM C CH2 TRP A 259 . −28.222 14.027 14.288 1.00 16.34 . 1 1983 ATOM N N THR A 260 . −30.814 8.661 18.835 1.00 11.58 . 1 1984 ATOM C CA THR A 260 . −31.794 7.980 19.639 1.00 11.95 . 1 1985 ATOM C C THR A 260 . −32.874 7.303 18.757 1.00 11.94 . 1 1986 ATOM O O THR A 260 . −33.027 7.593 17.551 1.00 13.21 . 1 1987 ATOM C CB THR A 260 . −32.528 8.954 20.528 1.00 12.69 . 1 1988 ATOM O OG1 THR A 260 . −33.158 9.920 19.648 1.00 13.35 . 1 1989 ATOM C CG2 THR A 260 . −31.543 9.644 21.579 1.00 13.80 . 1 1990 ATOM N N ASP A 261 . −33.659 6.418 19.355 1.00 13.72 . 1 1991 ATOM C CA ASP A 261 . −34.743 5.796 18.605 1.00 14.81 . 1 1992 ATOM C C ASP A 261 . −35.652 6.899 18.033 1.00 14.18 . 1 1993 ATOM O O ASP A 261 . −36.079 6.827 16.874 1.00 14.77 . 1 1994 ATOM C CB ASP A 261 . −35.610 4.948 19.526 1.00 15.37 . 1 1995 ATOM C CG ASP A 261 . −34.908 3.734 20.042 1.00 17.76 . 1 1996 ATOM O OD1 ASP A 261 . −33.770 3.451 19.632 1.00 17.47 . 1 1997 ATOM O OD2 ASP A 261 . −35.561 3.052 20.888 1.00 22.88 . 1 1998 ATOM N N LYS A 262 . −35.968 7.931 18.812 1.00 13.99 . 1 1999 ATOM C CA LYS A 262 . −36.854 8.992 18.309 1.00 16.20 . 1 2000 ATOM C C LYS A 262 . −36.267 9.683 17.043 1.00 12.99 . 1 2001 ATOM O O LYS A 262 . −36.962 9.930 16.040 1.00 14.51 . 1 2002 ATOM C CB LYS A 262 . −37.079 10.035 19.417 1.00 18.73 . 1 2003 ATOM C CG LYS A 262 . −37.884 11.219 18.960 1.00 23.64 . 1 2004 ATOM C CD LYS A 262 . −38.260 12.081 20.161 1.00 28.30 . 1 2005 ATOM C CE LYS A 262 . −39.395 13.045 19.805 1.00 31.35 . 1 2006 ATOM N NZ LYS A 262 . −40.131 13.401 21.085 1.00 35.95 . 1 2007 ATOM N N ASP A 263 . −34.983 10.017 17.092 1.00 12.28 . 1 2008 ATOM C CA ASP A 263 . −34.347 10.653 15.947 1.00 11.29 . 1 2009 ATOM C C ASP A 263 . −34.209 9.681 14.780 1.00 12.31 . 1 2010 ATOM O O ASP A 263 . −34.330 10.107 13.635 1.00 11.83 . 1 2011 ATOM C CB ASP A 263 . −33.002 11.245 16.357 1.00 13.50 . 1 2012 ATOM C CG ASP A 263 . −33.176 12.578 17.045 1.00 14.32 . 1 2013 ATOM O OD1 ASP A 263 . −34.237 13.207 16.808 1.00 15.84 . 1 2014 ATOM O OD2 ASP A 263 . −32.288 12.995 17.832 1.00 15.07 . 1 2015 ATOM N N CYS A 264 . −33.966 8.396 15.061 1.00 12.51 . 1 2016 ATOM C CA CYS A 264 . −33.863 7.417 13.960 1.00 12.90 . 1 2017 ATOM C C CYS A 264 . −35.189 7.345 13.262 1.00 12.38 . 1 2018 ATOM O O CYS A 264 . −35.245 7.231 12.025 1.00 12.29 . 1 2019 ATOM C CB CYS A 264 . −33.534 6.014 14.470 1.00 13.55 . 1 2020 ATOM S SG CYS A 264 . −31.738 5.863 14.813 1.00 13.94 . 1 2021 ATOM N N LEU A 265 . −36.296 7.412 14.015 1.00 11.87 . 1 2022 ATOM C CA LEU A 265 . −37.613 7.383 13.354 1.00 12.59 . 1 2023 ATOM C C LEU A 265 . −37.775 8.593 12.430 1.00 12.82 . 1 2024 ATOM O O LEU A 265 . −38.331 8.481 11.321 1.00 12.27 . 1 2025 ATOM C CB LEU A 265 . −38.775 7.346 14.367 1.00 13.50 . 1 2026 ATOM C CG LEU A 265 . −38.912 6.064 15.151 1.00 14.38 . 1 2027 ATOM C CD1 LEU A 265 . −40.012 6.241 16.161 1.00 15.36 . 1 2028 ATOM C CD2 LEU A 265 . −39.207 4.889 14.193 1.00 16.26 . 1 2029 ATOM N N ARG A 266 . −37.318 9.754 12.865 1.00 13.35 . 1 2030 ATOM C CA ARG A 266 . −37.413 10.916 11.984 1.00 12.93 . 1 2031 ATOM C C ARG A 266 . −36.611 10.697 10.680 1.00 11.37 . 1 2032 ATOM O O ARG A 266 . −37.094 10.965 9.557 1.00 12.53 . 1 2033 ATOM C CB ARG A 266 . −36.882 12.141 12.699 1.00 14.04 . 1 2034 ATOM C CG ARG A 266 . −37.729 12.524 13.926 1.00 16.48 . 1 2035 ATOM C CD ARG A 266 . −37.161 13.731 14.681 1.00 22.36 . 1 2036 ATOM N NE ARG A 266 . −38.079 14.060 15.775 1.00 30.96 . 1 2037 ATOM C CZ ARG A 266 . −37.782 14.919 16.752 1.00 33.68 . 1 2038 ATOM N NH1 ARG A 266 . −36.595 15.532 16.743 1.00 36.51 . 1 2039 ATOM N NH2 ARG A 266 . −38.640 15.137 17.752 1.00 34.89 . 1 2040 ATOM N N ILE A 267 . −35.369 10.236 10.783 1.00 11.71 . 1 2041 ATOM C CA ILE A 267 . −34.529 9.989 9.606 1.00 11.43 . 1 2042 ATOM C C ILE A 267 . −35.192 8.918 8.724 1.00 11.89 . 1 2043 ATOM O O ILE A 267 . −35.280 9.103 7.495 1.00 11.89 . 1 2044 ATOM C CB ILE A 267 . −33.117 9.459 10.037 1.00 11.02 . 1 2045 ATOM C CG1 ILE A 267 . −32.370 10.538 10.852 1.00 11.43 . 1 2046 ATOM C CG2 ILE A 267 . −32.305 8.974 8.801 1.00 10.61 . 1 2047 ATOM C CD1 ILE A 267 . −31.163 9.991 11.623 1.00 12.68 . 1 2048 ATOM N N LEU A 268 . −35.618 7.793 9.323 1.00 11.67 . 1 2049 ATOM C CA LEU A 268 . −36.225 6.714 8.532 1.00 11.75 . 1 2050 ATOM C C LEU A 268 . −37.486 7.204 7.788 1.00 12.90 . 1 2051 ATOM O O LEU A 268 . −37.735 6.741 6.652 1.00 13.34 . 1 2052 ATOM C CB LEU A 268 . −36.534 5.497 9.398 1.00 13.50 . 1 2053 ATOM C CG LEU A 268 . −35.292 4.734 9.829 1.00 13.31 . 1 2054 ATOM C CD1 LEU A 268 . −35.718 3.704 10.867 1.00 16.67 . 1 2055 ATOM C CD2 LEU A 268 . −34.647 4.051 8.601 1.00 14.68 . 1 2056 ATOM N N LYS A 269 . −38.289 8.093 8.390 1.00 11.61 . 1 2057 ATOM C CA LYS A 269 . −39.455 8.593 7.658 1.00 12.69 . 1 2058 ATOM C C LYS A 269 . −39.035 9.384 6.431 1.00 12.32 . 1 2059 ATOM O O LYS A 269 . −39.678 9.231 5.369 1.00 12.37 . 1 2060 ATOM C CB LYS A 269 . −40.319 9.480 8.578 1.00 14.85 . 1 2061 ATOM C CG LYS A 269 . −41.528 10.152 7.848 1.00 22.17 . 1 2062 ATOM C CD LYS A 269 . −42.362 10.983 8.845 1.00 27.16 . 1 2063 ATOM C CE LYS A 269 . −43.657 11.525 8.210 1.00 28.73 . 1 2064 ATOM N NZ LYS A 269 . −44.518 12.169 9.277 1.00 32.36 . 1 2065 ATOM N N LYS A 270 . −38.009 10.242 6.544 1.00 12.20 . 1 2066 ATOM C CA LYS A 270 . −37.538 11.002 5.409 1.00 12.38 . 1 2067 ATOM C C LYS A 270 . −36.914 10.089 4.351 1.00 11.57 . 1 2068 ATOM O O LYS A 270 . −37.029 10.353 3.151 1.00 11.98 . 1 2069 ATOM C CB LYS A 270 . −36.538 12.110 5.857 1.00 13.05 . 1 2070 ATOM C CG LYS A 270 . −37.213 13.223 6.698 1.00 14.47 . 1 2071 ATOM C CD LYS A 270 . −38.140 14.057 5.850 1.00 16.59 . 1 2072 ATOM C CE LYS A 270 . −38.822 15.169 6.706 1.00 18.14 . 1 2073 ATOM N NZ LYS A 270 . −39.748 15.930 5.843 1.00 21.48 . 1 2074 ATOM N N CYS A 271 . −36.290 8.998 4.789 1.00 11.88 . 1 2075 ATOM C CA CYS A 271 . −35.737 8.087 3.783 1.00 11.70 . 1 2076 ATOM C C CYS A 271 . −36.863 7.371 3.026 1.00 10.57 . 1 2077 ATOM O O CYS A 271 . −36.770 7.192 1.802 1.00 10.83 . 1 2078 ATOM C CB CYS A 271 . −34.817 7.039 4.429 1.00 12.30 . 1 2079 ATOM S SG CYS A 271 . −33.320 7.678 5.193 1.00 12.20 . 1 2080 ATOM N N LYS A 272 . −37.896 6.941 3.775 1.00 10.81 . 1 2081 ATOM C CA LYS A 272 . −39.034 6.256 3.148 1.00 12.65 . 1 2082 ATOM C C LYS A 272 . −39.660 7.195 2.109 1.00 12.84 . 1 2083 ATOM O O LYS A 272 . −39.995 6.767 0.968 1.00 13.03 . 1 2084 ATOM C CB LYS A 272 . −40.105 5.842 4.183 1.00 13.93 . 1 2085 ATOM C CG LYS A 272 . −41.292 5.120 3.527 1.00 15.50 . 1 2086 ATOM C CD LYS A 272 . −42.134 4.406 4.567 1.00 19.11 . 1 2087 ATOM C CE LYS A 272 . −42.841 5.366 5.409 1.00 24.41 . 1 2088 ATOM N NZ LYS A 272 . −43.499 4.592 6.515 1.00 29.89 . 1 2089 ATOM N N GLU A 273 . −39.820 8.452 2.490 1.00 12.93 . 1 2090 ATOM C CA GLU A 273 . −40.390 9.409 1.536 1.00 14.31 . 1 2091 ATOM C C GLU A 273 . −39.512 9.442 0.254 1.00 14.06 . 1 2092 ATOM O O GLU A 273 . −40.009 9.351 −0.873 1.00 14.49 . 1 2093 ATOM C CB GLU A 273 . −40.336 10.813 2.108 1.00 16.38 . 1 2094 ATOM C CG GLU A 273 . −41.394 11.275 3.012 1.00 25.67 . 1 2095 ATOM C CD GLU A 273 . −40.983 12.686 3.547 1.00 28.83 . 1 2096 ATOM O OE1 GLU A 273 . −40.312 13.491 2.761 1.00 27.17 . 1 2097 ATOM O OE2 GLU A 273 . −41.299 12.956 4.750 1.00 29.75 . 1 2098 ATOM N N ALA A 274 . −38.196 9.567 0.412 1.00 13.05 . 1 2099 ATOM C CA ALA A 274 . −37.289 9.678 −0.721 1.00 12.24 . 1 2100 ATOM C C ALA A 274 . −37.342 8.491 −1.703 1.00 12.93 . 1 2101 ATOM O O ALA A 274 . −37.050 8.665 −2.902 1.00 14.96 . 1 2102 ATOM C CB ALA A 274 . −35.837 9.883 −0.188 1.00 13.22 . 1 2103 ATOM N N VAL A 275 . −37.700 7.300 −1.206 1.00 12.04 . 1 2104 ATOM C CA VAL A 275 . −37.723 6.158 −2.099 1.00 13.64 . 1 2105 ATOM C C VAL A 275 . −39.106 5.715 −2.496 1.00 14.61 . 1 2106 ATOM O O VAL A 275 . −39.239 4.681 −3.160 1.00 15.21 . 1 2107 ATOM C CB VAL A 275 . −36.875 4.975 −1.511 1.00 12.32 . 1 2108 ATOM C CG1 VAL A 275 . −35.417 5.467 −1.240 1.00 11.89 . 1 2109 ATOM C CG2 VAL A 275 . −37.553 4.376 −0.281 1.00 12.77 . 1 2110 ATOM N N THR A 276 . −40.110 6.509 −2.151 1.00 15.87 . 1 2111 ATOM C CA THR A 276 . −41.494 6.171 −2.538 1.00 16.92 . 1 2112 ATOM C C THR A 276 . −42.186 7.295 −3.333 1.00 18.99 . 1 2113 ATOM O O THR A 276 . −43.414 7.258 −3.504 1.00 21.35 . 1 2114 ATOM C CB THR A 276 . −42.374 5.809 −1.323 1.00 16.69 . 1 2115 ATOM O OG1 THR A 276 . −42.341 6.850 −0.344 1.00 17.70 . 1 2116 ATOM C CG2 THR A 276 . −41.864 4.554 −0.668 1.00 18.64 . 1 2117 ATOM N N ASN A 277 . −41.421 8.270 −3.830 1.00 21.19 . 1 2118 ATOM C CA ASN A 277 . −41.974 9.385 −4.651 1.00 25.98 . 1 2119 ATOM C C ASN A 277 . −42.425 8.878 −6.054 1.00 28.21 . 1 2120 ATOM O O ASN A 277 . −41.960 7.842 −6.553 1.00 27.56 . 1 2121 ATOM C CB ASN A 277 . −40.904 10.483 −4.896 1.00 28.33 . 1 2122 ATOM C CG ASN A 277 . −41.384 11.610 −5.845 1.00 32.88 . 1 2123 ATOM O OD1 ASN A 277 . −41.959 12.627 −5.385 1.00 34.13 . 1 2124 ATOM N ND2 ASN A 277 . −41.137 11.451 −7.167 1.00 33.14 . 1 2125 ATOM N N ASP A 278 . −43.298 9.630 −6.705 1.00 30.51 . 1 2126 ATOM C CA ASP A 278 . −43.794 9.232 −8.017 1.00 33.84 . 1 2127 ATOM C C ASP A 278 . −44.171 7.737 −8.134 1.00 33.97 . 1 2128 ATOM O O ASP A 278 . −43.763 7.063 −9.093 1.00 36.87 . 1 2129 ATOM C CB ASP A 278 . −42.776 9.584 −9.123 1.00 36.44 . 1 2130 ATOM C CG ASP A 278 . −43.369 9.412 −10.543 1.00 38.89 . 1 2131 ATOM O OD1 ASP A 278 . −44.606 9.630 −10.713 1.00 40.37 . 1 2132 ATOM O OD2 ASP A 278 . −42.606 9.065 −11.484 1.00 39.51 . 1 2133 ATOM N N GLY A 279 . −44.944 7.228 −7.176 1.00 32.59 . 1 2134 ATOM C CA GLY A 279 . −45.377 5.839 −7.226 1.00 30.23 . 1 2135 ATOM C C GLY A 279 . −44.327 4.739 −7.127 1.00 28.82 . 1 2136 ATOM O O GLY A 279 . −44.665 3.544 −7.125 1.00 28.98 . 1 2137 ATOM N N LYS A 280 . −43.056 5.114 −7.078 1.00 25.55 . 1 2138 ATOM C CA LYS A 280 . −41.990 4.100 −6.983 1.00 23.24 . 1 2139 ATOM C C LYS A 280 . −41.940 3.435 −5.616 1.00 20.19 . 1 2140 ATOM O O LYS A 280 . −42.457 3.984 −4.640 1.00 18.84 . 1 2141 ATOM C CB LYS A 280 . −40.635 4.730 −7.248 1.00 24.63 . 1 2142 ATOM C CG LYS A 280 . −40.483 5.301 −8.666 1.00 27.66 . 1 2143 ATOM C CD LYS A 280 . −39.248 6.196 −8.693 1.00 29.71 . 1 2144 ATOM C CE LYS A 280 . −39.027 6.885 −10.064 1.00 31.41 . 1 2145 ATOM N NZ LYS A 280 . −38.530 5.962 −11.122 1.00 33.09 . 1 2146 ATOM N N ARG A 281 . −41.308 2.255 −5.557 1.00 17.22 . 1 2147 ATOM C CA ARG A 281 . −41.185 1.524 −4.292 1.00 15.66 . 1 2148 ATOM C C ARG A 281 . −39.756 1.056 −4.209 1.00 16.00 . 1 2149 ATOM O O ARG A 281 . −39.433 −0.061 −4.559 1.00 16.92 . 1 2150 ATOM C CB ARG A 281 . −42.122 0.315 −4.302 1.00 19.23 . 1 2151 ATOM C CG ARG A 281 . −43.536 0.670 −4.647 1.00 22.27 . 1 2152 ATOM C CD ARG A 281 . −44.108 1.585 −3.654 1.00 23.31 . 1 2153 ATOM N NE ARG A 281 . −44.006 1.049 −2.314 1.00 22.68 . 1 2154 ATOM C CZ ARG A 281 . −44.432 1.708 −1.253 1.00 24.78 . 1 2155 ATOM N NH1 ARG A 281 . −44.978 2.920 −1.388 1.00 24.93 . 1 2156 ATOM N NH2 ARG A 281 . −44.306 1.177 −0.047 1.00 24.51 . 1 2157 ATOM N N GLY A 282 . −38.888 1.938 −3.703 1.00 12.90 . 1 2158 ATOM C CA GLY A 282 . −37.478 1.617 −3.570 1.00 12.16 . 1 2159 ATOM C C GLY A 282 . −37.146 0.939 −2.245 1.00 12.64 . 1 2160 ATOM O O GLY A 282 . −37.987 0.280 −1.615 1.00 14.10 . 1 2161 ATOM N N LYS A 283 . −35.918 1.156 −1.760 1.00 12.60 . 1 2162 ATOM C CA LYS A 283 . −35.525 0.539 −0.509 1.00 12.34 . 1 2163 ATOM C C LYS A 283 . −34.454 1.383 0.201 1.00 12.65 . 1 2164 ATOM O O LYS A 283 . −33.897 2.328 −0.377 1.00 12.92 . 1 2165 ATOM C CB LYS A 283 . −34.957 −0.860 −0.808 1.00 13.16 . 1 2166 ATOM C CG LYS A 283 . −33.698 −0.779 −1.648 1.00 16.31 . 1 2167 ATOM C CD LYS A 283 . −32.874 −1.980 −1.608 1.00 21.02 . 1 2168 ATOM C CE LYS A 283 . −31.621 −1.724 −2.507 1.00 18.98 . 1 2169 ATOM N NZ LYS A 283 . −31.026 −3.020 −2.709 1.00 21.68 . 1 2170 ATOM N N VAL A 284 . −34.172 0.971 1.447 1.00 11.83 . 1 2171 ATOM C CA VAL A 284 . −33.153 1.656 2.262 1.00 11.32 . 1 2172 ATOM C C VAL A 284 . −32.158 0.607 2.711 1.00 10.11 . 1 2173 ATOM O O VAL A 284 . −32.532 −0.482 3.167 1.00 11.97 . 1 2174 ATOM C CB VAL A 284 . −33.817 2.358 3.471 1.00 10.54 . 1 2175 ATOM C CG1 VAL A 284 . −32.745 3.006 4.321 1.00 11.28 . 1 2176 ATOM C CG2 VAL A 284 . −34.740 3.472 2.976 1.00 10.28 . 1 2177 ATOM N N THR A 285 . −30.886 0.875 2.517 1.00 10.09 . 1 2178 ATOM C CA THR A 285 . −29.790 −0.027 2.887 1.00 10.30 . 1 2179 ATOM C C THR A 285 . −29.001 0.613 4.010 1.00 11.49 . 1 2180 ATOM O O THR A 285 . −28.563 1.734 3.862 1.00 12.24 . 1 2181 ATOM C CB THR A 285 . −28.877 −0.249 1.655 1.00 11.93 . 1 2182 ATOM O OG1 THR A 285 . −29.659 −0.823 0.581 1.00 13.44 . 1 2183 ATOM C CG2 THR A 285 . −27.714 −1.150 1.976 1.00 13.24 . 1 2184 ATOM N N ILE A 286 . −28.842 −0.124 5.099 1.00 11.16 . 1 2185 ATOM C CA ILE A 286 . −28.199 0.364 6.324 1.00 10.52 . 1 2186 ATOM C C ILE A 286 . −26.941 −0.479 6.613 1.00 11.64 . 1 2187 ATOM O O ILE A 286 . −26.979 −1.700 6.493 1.00 12.24 . 1 2188 ATOM C CB ILE A 286 . −29.159 0.155 7.520 1.00 10.69 . 1 2189 ATOM C CG1 ILE A 286 . −30.330 1.141 7.412 1.00 10.78 . 1 2190 ATOM C CG2 ILE A 286 . −28.463 0.341 8.871 1.00 11.59 . 1 2191 ATOM C CD1 ILE A 286 . −31.569 0.668 8.159 1.00 11.89 . 1 2192 ATOM N N ILE A 287 . −25.851 0.187 6.982 1.00 10.30 . 1 2193 ATOM C CA ILE A 287 . −24.627 −0.497 7.432 1.00 11.62 . 1 2194 ATOM C C ILE A 287 . −24.375 −0.010 8.854 1.00 13.49 . 1 2195 ATOM O O ILE A 287 . −24.188 1.185 9.077 1.00 11.80 . 1 2196 ATOM C CB ILE A 287 . −23.416 −0.183 6.557 1.00 11.13 . 1 2197 ATOM C CG1 ILE A 287 . −23.606 −0.794 5.147 1.00 12.94 . 1 2198 ATOM C CG2 ILE A 287 . −22.154 −0.766 7.222 1.00 11.65 . 1 2199 ATOM C CD1 ILE A 287 . −22.515 −0.422 4.172 1.00 12.51 . 1 2200 ATOM N N ASP A 288 . −24.455 −0.937 9.819 1.00 12.09 . 1 2201 ATOM C CA ASP A 288 . −24.211 −0.650 11.269 1.00 12.48 . 1 2202 ATOM C C ASP A 288 . −24.152 −2.008 11.963 1.00 12.57 . 1 2203 ATOM O O ASP A 288 . −24.395 −3.075 11.323 1.00 12.81 . 1 2204 ATOM C CB ASP A 288 . −25.327 0.223 11.890 1.00 12.67 . 1 2205 ATOM C CG ASP A 288 . −24.932 1.732 12.076 1.00 11.54 . 1 2206 ATOM O OD1 ASP A 288 . −23.755 2.053 12.367 1.00 12.36 . 1 2207 ATOM O OD2 ASP A 288 . −25.855 2.582 11.966 1.00 12.73 . 1 2208 ATOM N N MET A 289 . −23.765 −1.983 13.238 1.00 13.79 . 1 2209 ATOM C CA MET A 289 . −23.701 −3.241 13.976 1.00 13.79 . 1 2210 ATOM C C MET A 289 . −25.057 −3.816 14.309 1.00 13.11 . 1 2211 ATOM O O MET A 289 . −26.061 −3.103 14.455 1.00 13.77 . 1 2212 ATOM C CB MET A 289 . −23.001 −3.035 15.326 1.00 13.43 . 1 2213 ATOM C CG MET A 289 . −21.574 −2.679 15.257 1.00 16.38 . 1 2214 ATOM S SD MET A 289 . −20.975 −2.330 17.005 1.00 17.00 . 1 2215 ATOM C CE MET A 289 . −19.242 −2.684 16.703 1.00 21.73 . 1 2216 ATOM N N VAL A 290 . −25.089 −5.150 14.469 1.00 15.19 . 1 2217 ATOM C CA VAL A 290 . −26.301 −5.818 14.942 1.00 14.93 . 1 2218 ATOM C C VAL A 290 . −25.805 −6.707 16.078 1.00 18.10 . 1 2219 ATOM O O VAL A 290 . −25.012 −7.645 15.833 1.00 18.68 . 1 2220 ATOM C CB VAL A 290 . −26.945 −6.734 13.892 1.00 16.64 . 1 2221 ATOM C CG1 VAL A 290 . −28.115 −7.510 14.543 1.00 17.75 . 1 2222 ATOM C CG2 VAL A 290 . −27.506 −5.885 12.732 1.00 16.61 . 1 2223 ATOM N N ILE A 291 . −26.220 −6.384 17.294 1.00 16.64 . 1 2224 ATOM C CA ILE A 291 . −25.843 −7.178 18.469 1.00 18.82 . 1 2225 ATOM C C ILE A 291 . −26.640 −8.472 18.406 1.00 20.57 . 1 2226 ATOM O O ILE A 291 . −27.811 −8.453 18.059 1.00 19.70 . 1 2227 ATOM C CB ILE A 291 . −26.146 −6.435 19.771 1.00 18.18 . 1 2228 ATOM C CG1 ILE A 291 . −25.121 −5.291 19.903 1.00 17.63 . 1 2229 ATOM C CG2 ILE A 291 . −26.125 −7.455 20.961 1.00 18.30 . 1 2230 ATOM C CD1 ILE A 291 . −25.188 −4.421 21.111 1.00 19.53 . 1 2231 ATOM N N ASP A 292 . −25.986 −9.605 18.714 1.00 21.73 . 1 2232 ATOM C CA ASP A 292 . −26.657 −10.905 18.709 1.00 24.18 . 1 2233 ATOM C C ASP A 292 . −25.895 −11.782 19.721 1.00 25.63 . 1 2234 ATOM O O ASP A 292 . −24.924 −12.453 19.371 1.00 24.05 . 1 2235 ATOM C CB ASP A 292 . −26.619 −11.541 17.310 1.00 26.40 . 1 2236 ATOM C CG ASP A 292 . −27.531 −12.738 17.202 1.00 28.92 . 1 2237 ATOM O OD1 ASP A 292 . −27.806 −13.371 18.247 1.00 30.95 . 1 2238 ATOM O OD2 ASP A 292 . −27.973 −13.054 16.078 1.00 30.67 . 1 2239 ATOM N N LYS A 293 . −26.337 −11.721 20.974 1.00 26.38 . 1 2240 ATOM C CA LYS A 293 . −25.690 −12.452 22.058 1.00 28.05 . 1 2241 ATOM C C LYS A 293 . −25.676 −13.952 21.857 1.00 30.15 . 1 2242 ATOM O O LYS A 293 . −24.777 −14.645 22.327 1.00 30.24 . 1 2243 ATOM C CB LYS A 293 . −26.364 −12.127 23.392 1.00 27.39 . 1 2244 ATOM C CG LYS A 293 . −26.362 −10.633 23.753 1.00 27.53 . 1 2245 ATOM C CD LYS A 293 . −27.056 −10.403 25.110 1.00 29.13 . 1 2246 ATOM C CE LYS A 293 . −26.899 −8.955 25.608 1.00 28.60 . 1 2247 ATOM N NZ LYS A 293 . −27.582 −8.724 26.946 1.00 30.84 . 1 2248 ATOM N N LYS A 294 . −26.637 −14.475 21.133 1.00 31.94 . 1 2249 ATOM C CA LYS A 294 . −26.610 −15.915 20.993 1.00 33.89 . 1 2250 ATOM C C LYS A 294 . −25.866 −16.429 19.781 1.00 33.98 . 1 2251 ATOM O O LYS A 294 . −25.446 −17.585 19.760 1.00 34.96 . 1 2252 ATOM C CB LYS A 294 . −28.024 −16.464 21.020 1.00 35.98 . 1 2253 ATOM C CG LYS A 294 . −29.031 −15.669 20.239 1.00 38.30 . 1 2254 ATOM C CD LYS A 294 . −30.420 −15.929 20.820 1.00 40.84 . 1 2255 ATOM C CE LYS A 294 . −31.375 −14.748 20.518 1.00 41.17 . 1 2256 ATOM N NZ LYS A 294 . −32.725 −14.987 21.170 1.00 42.67 . 1 2257 ATOM N N LYS A 295 . −25.666 −15.587 18.779 1.00 33.77 . 1 2258 ATOM C CA LYS A 295 . −24.981 −16.031 17.568 1.00 33.32 . 1 2259 ATOM C C LYS A 295 . −23.530 −15.626 17.492 1.00 32.56 . 1 2260 ATOM O O LYS A 295 . −22.694 −16.374 16.983 1.00 31.78 . 1 2261 ATOM C CB LYS A 295 . −25.685 −15.476 16.328 1.00 35.27 . 1 2262 ATOM C CG LYS A 295 . −27.178 −15.664 16.351 1.00 37.45 . 1 2263 ATOM C CD LYS A 295 . −27.578 −17.136 16.318 1.00 39.38 . 1 2264 ATOM C CE LYS A 295 . −29.073 −17.256 16.593 1.00 40.37 . 1 2265 ATOM N NZ LYS A 295 . −29.622 −18.658 16.458 1.00 42.48 . 1 2266 ATOM N N ASP A 296 . −23.235 −14.416 17.941 1.00 29.89 . 1 2267 ATOM C CA ASP A 296 . −21.881 −13.921 17.896 1.00 29.72 . 1 2268 ATOM C C ASP A 296 . −21.019 −14.618 18.919 1.00 29.92 . 1 2269 ATOM O O ASP A 296 . −21.511 −15.100 19.941 1.00 29.43 . 1 2270 ATOM C CB ASP A 296 . −21.826 −12.416 18.205 1.00 28.77 . 1 2271 ATOM C CG ASP A 296 . −22.301 −11.559 17.056 1.00 28.99 . 1 2272 ATOM O OD1 ASP A 296 . −22.535 −12.113 15.968 1.00 29.94 . 1 2273 ATOM O OD2 ASP A 296 . −22.425 −10.324 17.242 1.00 26.78 . 1 2274 ATOM N N GLU A 297 . −19.729 −14.635 18.616 1.00 30.30 . 1 2275 ATOM C CA GLU A 297 . −18.723 −15.179 19.488 1.00 31.45 . 1 2276 ATOM C C GLU A 297 . −18.710 −14.199 20.642 1.00 30.73 . 1 2277 ATOM O O GLU A 297 . −18.924 −12.991 20.438 1.00 30.13 . 1 2278 ATOM C CB GLU A 297 . −17.376 −15.175 18.768 1.00 34.40 . 1 2279 ATOM C CG GLU A 297 . −16.162 −15.174 19.674 1.00 38.60 . 1 2280 ATOM C CD GLU A 297 . −14.987 −15.823 18.977 1.00 41.63 . 1 2281 ATOM O OE1 GLU A 297 . −15.145 −17.037 18.654 1.00 44.26 . 1 2282 ATOM O OE2 GLU A 297 . −13.939 −15.139 18.744 1.00 42.99 . 1 2283 ATOM N N ASN A 298 . −18.453 −14.685 21.844 1.00 29.88 . 1 2284 ATOM C CA ASN A 298 . −18.484 −13.790 22.986 1.00 30.52 . 1 2285 ATOM C C ASN A 298 . −17.619 −12.573 22.857 1.00 29.97 . 1 2286 ATOM O O ASN A 298 . −18.049 −11.484 23.217 1.00 29.26 . 1 2287 ATOM C CB ASN A 298 . −18.118 −14.504 24.286 1.00 32.41 . 1 2288 ATOM C CG ASN A 298 . −18.201 −13.562 25.513 1.00 34.95 . 1 2289 ATOM O OD1 ASN A 298 . −17.243 −13.451 26.287 1.00 37.04 . 1 2290 ATOM N ND2 ASN A 298 . −19.347 −12.880 25.685 1.00 34.68 . 1 2291 ATOM N N GLN A 299 . −16.388 −12.746 22.390 1.00 28.80 . 1 2292 ATOM C CA GLN A 299 . −15.475 −11.631 22.235 1.00 28.22 . 1 2293 ATOM C C GLN A 299 . −16.109 −10.530 21.356 1.00 26.89 . 1 2294 ATOM O O GLN A 299 . −15.968 −9.342 21.654 1.00 26.63 . 1 2295 ATOM C CB GLN A 299 . −14.166 −12.112 21.588 1.00 31.01 . 1 2296 ATOM C CG GLN A 299 . −13.196 −10.998 21.122 1.00 34.66 . 1 2297 ATOM C CD GLN A 299 . −12.171 −11.476 20.041 1.00 37.45 . 1 2298 ATOM O OE1 GLN A 299 . −12.476 −11.541 18.833 1.00 39.12 . 1 2299 ATOM N NE2 GLN A 299 . −10.962 −11.807 20.487 1.00 39.02 . 1 2300 ATOM N N VAL A 300 . −16.778 −10.948 20.289 1.00 24.01 . 1 2301 ATOM C CA VAL A 300 . −17.411 −10.004 19.387 1.00 23.09 . 1 2302 ATOM C C VAL A 300 . −18.573 −9.292 20.076 1.00 21.89 . 1 2303 ATOM O O VAL A 300 . −18.737 −8.058 19.944 1.00 21.70 . 1 2304 ATOM C CB VAL A 300 . −17.922 −10.698 18.121 1.00 23.82 . 1 2305 ATOM C CG1 VAL A 300 . −18.648 −9.679 17.265 1.00 25.17 . 1 2306 ATOM C CG2 VAL A 300 . −16.759 −11.320 17.366 1.00 25.44 . 1 2307 ATOM N N THR A 301 . −19.406 −10.051 20.783 1.00 19.52 . 1 2308 ATOM C CA THR A 301 . −20.522 −9.442 21.527 1.00 17.90 . 1 2309 ATOM C C THR A 301 . −19.978 −8.415 22.521 1.00 17.14 . 1 2310 ATOM O O THR A 301 . −20.538 −7.314 22.657 1.00 16.48 . 1 2311 ATOM C CB THR A 301 . −21.338 −10.536 22.296 1.00 15.09 . 1 2312 ATOM O OG1 THR A 301 . −22.064 −11.331 21.335 1.00 18.96 . 1 2313 ATOM C CG2 THR A 301 . −22.281 −9.934 23.273 1.00 17.99 . 1 2314 ATOM N N GLN A 302 . −18.882 −8.724 23.202 1.00 18.85 . 1 2315 ATOM C CA GLN A 302 . −18.357 −7.771 24.167 1.00 17.73 . 1 2316 ATOM C C GLN A 302 . −17.909 −6.435 23.563 1.00 19.93 . 1 2317 ATOM O O GLN A 302 . −18.067 −5.368 24.189 1.00 20.61 . 1 2318 ATOM C CB GLN A 302 . −17.207 −8.426 24.924 1.00 19.98 . 1 2319 ATOM C CG GLN A 302 . −17.683 −9.565 25.831 1.00 22.06 . 1 2320 ATOM C CD GLN A 302 . −18.793 −9.111 26.759 1.00 22.63 . 1 2321 ATOM O OE1 GLN A 302 . −18.688 −8.050 27.389 1.00 24.87 . 1 2322 ATOM N NE2 GLN A 302 . −19.869 −9.889 26.847 1.00 24.81 . 1 2323 ATOM N N ILE A 303 . −17.309 −6.476 22.386 1.00 20.60 . 1 2324 ATOM C CA ILE A 303 . −16.903 −5.223 21.747 1.00 20.93 . 1 2325 ATOM C C ILE A 303 . −18.156 −4.430 21.312 1.00 19.18 . 1 2326 ATOM O O ILE A 303 . −18.193 −3.211 21.434 1.00 18.55 . 1 2327 ATOM C CB ILE A 303 . −16.027 −5.461 20.484 1.00 22.20 . 1 2328 ATOM C CG1 ILE A 303 . −14.640 −6.039 20.881 1.00 25.11 . 1 2329 ATOM C CG2 ILE A 303 . −15.853 −4.147 19.708 1.00 23.70 . 1 2330 ATOM C CD1 ILE A 303 . −13.949 −5.336 21.998 1.00 25.40 . 1 2331 ATOM N N LYS A 304 . −19.164 −5.121 20.789 1.00 17.58 . 1 2332 ATOM C CA LYS A 304 . −20.384 −4.422 20.387 1.00 15.76 . 1 2333 ATOM C C LYS A 304 . −21.067 −3.738 21.589 1.00 16.67 . 1 2334 ATOM O O LYS A 304 . −21.532 −2.586 21.486 1.00 15.10 . 1 2335 ATOM C CB LYS A 304 . −21.356 −5.365 19.648 1.00 17.47 . 1 2336 ATOM C CG LYS A 304 . −20.804 −5.895 18.329 1.00 16.87 . 1 2337 ATOM C CD LYS A 304 . −21.828 −6.694 17.586 1.00 16.88 . 1 2338 ATOM C CE LYS A 304 . −21.242 −7.232 16.232 1.00 16.92 . 1 2339 ATOM N NZ LYS A 304 . −22.199 −8.105 15.486 1.00 19.52 . 1 2340 ATOM N N LEU A 305 . −21.098 −4.427 22.723 1.00 16.34 . 1 2341 ATOM C CA LEU A 305 . −21.685 −3.895 23.937 1.00 15.98 . 1 2342 ATOM C C LEU A 305 . −20.856 −2.712 24.420 1.00 13.61 . 1 2343 ATOM O O LEU A 305 . −21.372 −1.719 24.947 1.00 14.99 . 1 2344 ATOM C CB LEU A 305 . −21.732 −4.942 25.055 1.00 16.35 . 1 2345 ATOM C CG LEU A 305 . −22.754 −6.036 24.803 1.00 16.53 . 1 2346 ATOM C CD1 LEU A 305 . −22.547 −7.174 25.829 1.00 14.88 . 1 2347 ATOM C CD2 LEU A 305 . −24.173 −5.470 24.930 1.00 17.65 . 1 2348 ATOM N N LEU A 306 . −19.535 −2.788 24.216 1.00 15.60 . 1 2349 ATOM C CA LEU A 306 . −18.679 −1.702 24.624 1.00 15.55 . 1 2350 ATOM C C LEU A 306 . −18.920 −0.472 23.698 1.00 16.74 . 1 2351 ATOM O O LEU A 306 . −18.996 0.673 24.178 1.00 15.19 . 1 2352 ATOM C CB LEU A 306 . −17.225 −2.157 24.499 1.00 19.18 . 1 2353 ATOM C CG LEU A 306 . −16.186 −1.047 24.496 1.00 19.00 . 1 2354 ATOM C CD1 LEU A 306 . −16.138 −0.328 25.862 1.00 19.57 . 1 2355 ATOM C CD2 LEU A 306 . −14.827 −1.739 24.128 1.00 22.97 . 1 2356 ATOM N N MET A 307 . −19.065 −0.717 22.393 1.00 17.23 . 1 2357 ATOM C CA MET A 307 . −19.343 0.397 21.473 1.00 18.19 . 1 2358 ATOM C C MET A 307 . −20.691 1.026 21.858 1.00 17.00 . 1 2359 ATOM O O MET A 307 . −20.872 2.253 21.763 1.00 14.70 . 1 2360 ATOM C CB MET A 307 . −19.425 −0.096 20.016 1.00 20.58 . 1 2361 ATOM C CG MET A 307 . −18.121 −0.323 19.300 1.00 26.11 . 1 2362 ATOM S SD MET A 307 . −17.138 1.215 19.028 1.00 33.45 . 1 2363 ATOM C CE MET A 307 . −18.200 2.304 18.883 1.00 13.20 . 1 2364 ATOM N N ASP A 308 . −21.642 0.180 22.279 1.00 14.42 . 1 2365 ATOM C CA ASP A 308 . −22.959 0.722 22.657 1.00 14.46 . 1 2366 ATOM C C ASP A 308 . −22.828 1.705 23.826 1.00 14.06 . 1 2367 ATOM O O ASP A 308 . −23.429 2.795 23.849 1.00 13.60 . 1 2368 ATOM C CB ASP A 308 . −23.937 −0.411 22.997 1.00 13.89 . 1 2369 ATOM C CG ASP A 308 . −25.237 0.116 23.541 1.00 16.53 . 1 2370 ATOM O OD1 ASP A 308 . −26.003 0.722 22.782 1.00 15.80 . 1 2371 ATOM O OD2 ASP A 308 . −25.503 −0.034 24.749 1.00 18.19 . 1 2372 ATOM N N VAL A 309 . −22.013 1.343 24.819 1.00 13.84 . 1 2373 ATOM C CA VAL A 309 . −21.854 2.267 25.923 1.00 14.44 . 1 2374 ATOM C C VAL A 309 . −21.138 3.531 25.459 1.00 14.71 . 1 2375 ATOM O O VAL A 309 . −21.465 4.647 25.843 1.00 14.29 . 1 2376 ATOM C CB VAL A 309 . −21.071 1.588 27.096 1.00 14.37 . 1 2377 ATOM C CG1 VAL A 309 . −20.633 2.665 28.056 1.00 16.56 . 1 2378 ATOM C CG2 VAL A 309 . −21.937 0.551 27.783 1.00 16.83 . 1 2379 ATOM N N ASN A 310 . −20.140 3.365 24.603 1.00 13.63 . 1 2380 ATOM C CA ASN A 310 . −19.396 4.519 24.073 1.00 14.59 . 1 2381 ATOM C C ASN A 310 . −20.279 5.530 23.305 1.00 14.67 . 1 2382 ATOM O O ASN A 310 . −19.976 6.692 23.275 1.00 14.54 . 1 2383 ATOM C CB ASN A 310 . −18.284 3.999 23.135 1.00 16.38 . 1 2384 ATOM C CG ASN A 310 . −17.554 5.108 22.405 1.00 15.62 . 1 2385 ATOM O OD1 ASN A 310 . −17.613 5.232 21.152 1.00 20.47 . 1 2386 ATOM N ND2 ASN A 310 . −16.912 5.955 23.144 1.00 14.82 . 1 2387 ATOM N N MET A 311 . −21.364 5.042 22.709 1.00 14.19 . 1 2388 ATOM C CA MET A 311 . −22.238 5.936 21.940 1.00 15.04 . 1 2389 ATOM C C MET A 311 . −23.006 6.980 22.745 1.00 14.64 . 1 2390 ATOM O O MET A 311 . −23.736 7.791 22.159 1.00 14.35 . 1 2391 ATOM C CB MET A 311 . −23.189 5.126 21.062 1.00 15.18 . 1 2392 ATOM C CG MET A 311 . −22.493 4.422 19.898 1.00 14.84 . 1 2393 ATOM S SD MET A 311 . −21.255 5.397 18.938 1.00 20.06 . 1 2394 ATOM C CE MET A 311 . −22.354 6.508 18.282 1.00 20.88 . 1 2395 ATOM N N ALA A 312 . −22.807 6.990 24.073 1.00 15.37 . 1 2396 ATOM C CA ALA A 312 . −23.382 7.996 24.957 1.00 14.30 . 1 2397 ATOM C C ALA A 312 . −22.969 9.362 24.401 1.00 13.39 . 1 2398 ATOM O O ALA A 312 . −23.660 10.346 24.553 1.00 14.29 . 1 2399 ATOM C CB ALA A 312 . −22.797 7.847 26.421 1.00 14.19 . 1 2400 ATOM N N CYS A 313 . −21.797 9.424 23.763 1.00 13.78 . 1 2401 ATOM C CA CYS A 313 . −21.309 10.672 23.166 1.00 14.13 . 1 2402 ATOM C C CYS A 313 . −22.378 11.394 22.338 1.00 14.30 . 1 2403 ATOM O O CYS A 313 . −22.451 12.606 22.357 1.00 14.74 . 1 2404 ATOM C CB CYS A 313 . −20.075 10.437 22.258 1.00 14.46 . 1 2405 ATOM S SG CYS A 313 . −20.268 9.239 20.835 1.00 14.49 . 1 2406 ATOM N N LEU A 314 . −23.179 10.637 21.577 1.00 13.80 . 1 2407 ATOM C CA LEU A 314 . −24.218 11.259 20.733 1.00 13.34 . 1 2408 ATOM C C LEU A 314 . −25.623 10.762 21.082 1.00 13.84 . 1 2409 ATOM O O LEU A 314 . −26.555 10.882 20.264 1.00 14.10 . 1 2410 ATOM C CB LEU A 314 . −23.921 10.903 19.255 1.00 14.28 . 1 2411 ATOM C CG LEU A 314 . −22.578 11.337 18.724 1.00 15.86 . 1 2412 ATOM C CD1 LEU A 314 . −22.268 10.821 17.272 1.00 17.79 . 1 2413 ATOM C CD2 LEU A 314 . −22.610 12.870 18.728 1.00 19.04 . 1 2414 ATOM N N ASN A 315 . −25.797 10.163 22.262 1.00 13.06 . 1 2415 ATOM C CA ASN A 315 . −27.078 9.560 22.682 1.00 13.04 . 1 2416 ATOM C C ASN A 315 . −27.377 8.453 21.663 1.00 11.97 . 1 2417 ATOM O O ASN A 315 . −28.525 8.112 21.410 1.00 13.45 . 1 2418 ATOM C CB ASN A 315 . −28.246 10.566 22.732 1.00 13.96 . 1 2419 ATOM C CG ASN A 315 . −28.215 11.433 23.974 1.00 16.49 . 1 2420 ATOM O OD1 ASN A 315 . −28.951 12.454 24.070 1.00 18.25 . 1 2421 ATOM N ND2 ASN A 315 . −27.404 11.030 24.955 1.00 13.03 . 1 2422 ATOM N N GLY A 316 . −26.319 7.883 21.093 1.00 12.67 . 1 2423 ATOM C CA GLY A 316 . −26.510 6.798 20.128 1.00 12.43 . 1 2424 ATOM C C GLY A 316 . −26.677 5.441 20.803 1.00 13.25 . 1 2425 ATOM O O GLY A 316 . −26.812 5.319 22.055 1.00 14.18 . 1 2426 ATOM N N LYS A 317 . −26.653 4.387 19.991 1.00 12.65 . 1 2427 ATOM C CA LYS A 317 . −26.894 3.034 20.483 1.00 13.30 . 1 2428 ATOM C C LYS A 317 . −26.479 1.990 19.459 1.00 13.62 . 1 2429 ATOM O O LYS A 317 . −26.522 2.297 18.247 1.00 13.30 . 1 2430 ATOM C CB LYS A 317 . −28.420 2.880 20.798 1.00 17.71 . 1 2431 ATOM C CG LYS A 317 . −28.901 1.482 21.238 1.00 17.87 . 1 2432 ATOM C CD LYS A 317 . −30.439 1.351 21.261 1.00 22.22 . 1 2433 ATOM C CE LYS A 317 . −31.133 2.344 22.127 1.00 22.77 . 1 2434 ATOM N NZ LYS A 317 . −32.537 1.859 22.372 1.00 28.37 . 1 2435 ATOM N N GLU A 318 . −26.018 0.810 19.890 1.00 14.03 . 1 2436 ATOM C CA GLU A 318 . −25.771 −0.275 18.932 1.00 15.46 . 1 2437 ATOM C C GLU A 318 . −26.921 −1.192 19.237 1.00 16.61 . 1 2438 ATOM O O GLU A 318 . −27.156 −1.558 20.397 1.00 18.91 . 1 2439 ATOM C CB GLU A 318 . −24.411 −0.941 19.118 1.00 15.12 . 1 2440 ATOM C CG GLU A 318 . −23.261 0.025 18.988 1.00 15.94 . 1 2441 ATOM C CD GLU A 318 . −23.101 0.710 17.620 1.00 13.47 . 1 2442 ATOM O OE1 GLU A 318 . −23.746 0.277 16.633 1.00 13.32 . 1 2443 ATOM O OE2 GLU A 318 . −22.311 1.688 17.514 1.00 14.16 . 1 2444 ATOM N N ARG A 319 . −27.655 −1.581 18.214 1.00 15.25 . 1 2445 ATOM C CA ARG A 319 . −28.887 −2.297 18.409 1.00 14.03 . 1 2446 ATOM C C ARG A 319 . −28.890 −3.772 18.094 1.00 14.64 . 1 2447 ATOM O O ARG A 319 . −28.182 −4.217 17.220 1.00 13.70 . 1 2448 ATOM C CB ARG A 319 . −29.970 −1.579 17.549 1.00 14.23 . 1 2449 ATOM C CG ARG A 319 . −30.348 −0.140 18.070 1.00 13.22 . 1 2450 ATOM C CD ARG A 319 . −31.190 0.682 17.033 1.00 13.65 . 1 2451 ATOM N NE ARG A 319 . −31.605 1.971 17.594 1.00 13.30 . 1 2452 ATOM C CZ ARG A 319 . −31.036 3.158 17.411 1.00 13.06 . 1 2453 ATOM N NH1 ARG A 319 . −29.955 3.334 16.642 1.00 12.04 . 1 2454 ATOM N NH2 ARG A 319 . −31.564 4.183 18.069 1.00 14.06 . 1 2455 ATOM N N ASN A 320 . −29.739 −4.496 18.816 1.00 16.38 . 1 2456 ATOM C CA ASN A 320 . −29.884 −5.904 18.500 1.00 16.18 . 1 2457 ATOM C C ASN A 320 . −31.022 −6.026 17.471 1.00 16.78 . 1 2458 ATOM O O ASN A 320 . −31.623 −4.993 17.115 1.00 16.48 . 1 2459 ATOM C CB ASN A 320 . −30.153 −6.760 19.749 1.00 16.19 . 1 2460 ATOM C CG ASN A 320 . −31.438 −6.405 20.467 1.00 16.60 . 1 2461 ATOM O OD1 ASN A 320 . −32.431 −6.040 19.877 1.00 18.44 . 1 2462 ATOM N ND2 ASN A 320 . −31.430 −6.575 21.787 1.00 19.36 . 1 2463 ATOM N N GLU A 321 . −31.283 −7.235 16.953 1.00 17.70 . 1 2464 ATOM C CA GLU A 321 . −32.321 −7.396 15.935 1.00 17.95 . 1 2465 ATOM C C GLU A 321 . −33.708 −6.968 16.361 1.00 17.69 . 1 2466 ATOM O O GLU A 321 . −34.397 −6.311 15.574 1.00 18.55 . 1 2467 ATOM C CB GLU A 321 . −32.355 −8.829 15.374 1.00 16.43 . 1 2468 ATOM C CG GLU A 321 . −33.422 −9.006 14.314 1.00 18.12 . 1 2469 ATOM C CD GLU A 321 . −33.298 −10.314 13.517 1.00 19.54 . 1 2470 ATOM O OE1 GLU A 321 . −32.289 −11.030 13.724 1.00 23.01 . 1 2471 ATOM O OE2 GLU A 321 . −34.208 −10.567 12.684 1.00 21.93 . 1 2472 ATOM N N GLU A 322 . −34.121 −7.231 17.594 1.00 18.11 . 1 2473 ATOM C CA GLU A 322 . −35.451 −6.799 18.018 1.00 18.82 . 1 2474 ATOM C C GLU A 322 . −35.564 −5.289 18.085 1.00 17.19 . 1 2475 ATOM O O GLU A 322 . −36.630 −4.775 17.815 1.00 17.12 . 1 2476 ATOM C CB GLU A 322 . −35.822 −7.405 19.373 1.00 23.09 . 1 2477 ATOM C CG GLU A 322 . −36.239 −8.912 19.202 1.00 27.98 . 1 2478 ATOM C CD GLU A 322 . −37.513 −9.116 18.315 1.00 31.56 . 1 2479 ATOM O OE1 GLU A 322 . −37.572 −10.087 17.503 1.00 34.36 . 1 2480 ATOM O OE2 GLU A 322 . −38.474 −8.320 18.436 1.00 32.04 . 1 2481 ATOM N N GLU A 323 . −34.477 −4.598 18.457 1.00 15.83 . 1 2482 ATOM C CA GLU A 323 . −34.500 −3.144 18.520 1.00 16.30 . 1 2483 ATOM C C GLU A 323 . −34.596 −2.562 17.094 1.00 15.72 . 1 2484 ATOM O O GLU A 323 . −35.384 −1.641 16.827 1.00 16.54 . 1 2485 ATOM C CB GLU A 323 . −33.258 −2.649 19.254 1.00 15.73 . 1 2486 ATOM C CG GLU A 323 . −33.344 −2.948 20.775 1.00 16.72 . 1 2487 ATOM C CD GLU A 323 . −32.033 −2.734 21.497 1.00 18.83 . 1 2488 ATOM O OE1 GLU A 323 . −30.980 −3.017 20.942 1.00 17.90 . 1 2489 ATOM O OE2 GLU A 323 . −32.108 −2.318 22.681 1.00 22.64 . 1 2490 ATOM N N TRP A 324 . −33.819 −3.125 16.173 1.00 16.59 . 1 2491 ATOM C CA TRP A 324 . −33.866 −2.696 14.778 1.00 15.93 . 1 2492 ATOM C C TRP A 324 . −35.270 −2.920 14.226 1.00 16.04 . 1 2493 ATOM O O TRP A 324 . −35.846 −2.014 13.643 1.00 15.40 . 1 2494 ATOM C CB TRP A 324 . −32.860 −3.489 13.939 1.00 15.66 . 1 2495 ATOM C CG TRP A 324 . −31.439 −3.034 14.045 1.00 15.09 . 1 2496 ATOM C CD1 TRP A 324 . −30.378 −3.758 14.442 1.00 13.87 . 1 2497 ATOM C CD2 TRP A 324 . −30.921 −1.755 13.635 1.00 12.88 . 1 2498 ATOM N NE1 TRP A 324 . −29.202 −3.022 14.308 1.00 13.26 . 1 2499 ATOM C CE2 TRP A 324 . −29.524 −1.781 13.806 1.00 12.36 . 1 2500 ATOM C CE3 TRP A 324 . −31.522 −0.581 13.132 1.00 13.78 . 1 2501 ATOM C CZ2 TRP A 324 . −28.693 −0.673 13.490 1.00 13.64 . 1 2502 ATOM C CZ3 TRP A 324 . −30.724 0.524 12.822 1.00 12.46 . 1 2503 ATOM C CH2 TRP A 324 . −29.313 0.480 12.999 1.00 13.11 . 1 2504 ATOM N N LYS A 325 . −35.811 −4.128 14.419 1.00 16.37 . 1 2505 ATOM C CA LYS A 325 . −37.156 −4.481 13.927 1.00 18.06 . 1 2506 ATOM C C LYS A 325 . −38.230 −3.505 14.431 1.00 18.32 . 1 2507 ATOM O O LYS A 325 . −39.058 −2.999 13.654 1.00 18.57 . 1 2508 ATOM C CB LYS A 325 . −37.508 −5.898 14.375 1.00 19.87 . 1 2509 ATOM C CG LYS A 325 . −38.877 −6.393 13.856 1.00 21.89 . 1 2510 ATOM C CD LYS A 325 . −39.096 −7.822 14.233 1.00 25.40 . 1 2511 ATOM C CE LYS A 325 . −40.484 −8.296 13.826 1.00 28.03 . 1 2512 ATOM N NZ LYS A 325 . −40.589 −9.777 14.104 1.00 31.22 . 1 2513 ATOM N N LYS A 326 . −38.186 −3.183 15.723 1.00 18.22 . 1 2514 ATOM C CA LYS A 326 . −39.162 −2.251 16.290 1.00 18.99 . 1 2515 ATOM C C LYS A 326 . −39.093 −0.865 15.617 1.00 18.64 . 1 2516 ATOM O O LYS A 326 . −40.113 −0.229 15.357 1.00 18.28 . 1 2517 ATOM C CB LYS A 326 . −38.923 −2.142 17.800 1.00 21.98 . 1 2518 ATOM C CG LYS A 326 . −39.970 −1.352 18.569 1.00 26.67 . 1 2519 ATOM C CD LYS A 326 . −39.535 −1.280 20.036 1.00 30.18 . 1 2520 ATOM C CE LYS A 326 . −40.335 −0.293 20.888 1.00 33.12 . 1 2521 ATOM N NZ LYS A 326 . −39.454 0.013 22.079 1.00 36.60 . 1 2522 ATOM N N LEU A 327 . −37.889 −0.400 15.291 1.00 16.34 . 1 2523 ATOM C CA LEU A 327 . −37.766 0.909 14.604 1.00 16.05 . 1 2524 ATOM C C LEU A 327 . −38.351 0.807 13.189 1.00 15.01 . 1 2525 ATOM O O LEU A 327 . −39.111 1.684 12.752 1.00 16.71 . 1 2526 ATOM C CB LEU A 327 . −36.315 1.371 14.425 1.00 17.37 . 1 2527 ATOM C CG LEU A 327 . −35.596 1.884 15.636 1.00 21.97 . 1 2528 ATOM C CD1 LEU A 327 . −34.157 2.200 15.268 1.00 23.53 . 1 2529 ATOM C CD2 LEU A 327 . −36.291 3.119 16.096 1.00 23.02 . 1 2530 ATOM N N PHE A 328 . −37.973 −0.258 12.483 1.00 14.87 . 1 2531 ATOM C CA PHE A 328 . −38.452 −0.408 11.086 1.00 14.87 . 1 2532 ATOM C C PHE A 328 . −39.967 −0.449 11.010 1.00 15.91 . 1 2533 ATOM O O PHE A 328 . −40.575 0.174 10.166 1.00 16.16 . 1 2534 ATOM C CB PHE A 328 . −37.866 −1.713 10.489 1.00 13.28 . 1 2535 ATOM C CG PHE A 328 . −36.360 −1.729 10.428 1.00 13.15 . 1 2536 ATOM C CD1 PHE A 328 . −35.683 −2.949 10.419 1.00 11.78 . 1 2537 ATOM C CD2 PHE A 328 . −35.616 −0.539 10.432 1.00 12.91 . 1 2538 ATOM C CE1 PHE A 328 . −34.255 −2.973 10.418 1.00 11.85 . 1 2539 ATOM C CE2 PHE A 328 . −34.240 −0.546 10.444 1.00 12.67 . 1 2540 ATOM C CZ PHE A 328 . −33.558 −1.734 10.440 1.00 13.24 . 1 2541 ATOM N N ILE A 329 . −40.565 −1.176 11.926 1.00 18.09 . 1 2542 ATOM C CA ILE A 329 . −42.017 −1.279 11.945 1.00 18.74 . 1 2543 ATOM C C ILE A 329 . −42.644 0.050 12.273 1.00 18.42 . 1 2544 ATOM O O ILE A 329 . −43.551 0.485 11.588 1.00 19.52 . 1 2545 ATOM C CB ILE A 329 . −42.435 −2.344 12.956 1.00 19.16 . 1 2546 ATOM C CG1 ILE A 329 . −42.040 −3.711 12.375 1.00 20.65 . 1 2547 ATOM C CG2 ILE A 329 . −43.931 −2.258 13.241 1.00 21.01 . 1 2548 ATOM C CD1 ILE A 329 . −42.235 −4.860 13.377 1.00 20.77 . 1 2549 ATOM N N GLU A 330 . −42.103 0.734 13.280 1.00 19.28 . 1 2550 ATOM C CA GLU A 330 . −42.681 2.006 13.658 1.00 20.49 . 1 2551 ATOM C C GLU A 330 . −42.501 3.031 12.557 1.00 19.36 . 1 2552 ATOM O O GLU A 330 . −43.325 3.936 12.429 1.00 20.30 . 1 2553 ATOM C CB GLU A 330 . −42.084 2.527 14.981 1.00 21.21 . 1 2554 ATOM C CG GLU A 330 . −42.871 3.712 15.487 1.00 27.12 . 1 2555 ATOM C CD GLU A 330 . −42.614 4.094 16.958 1.00 30.54 . 1 2556 ATOM O OE1 GLU A 330 . −41.799 3.423 17.657 1.00 32.07 . 1 2557 ATOM O OE2 GLU A 330 . −43.270 5.084 17.395 1.00 33.70 . 1 2558 ATOM N N ALA A 331 . −41.449 2.909 11.735 1.00 16.84 . 1 2559 ATOM C CA ALA A 331 . −41.260 3.857 10.641 1.00 18.03 . 1 2560 ATOM C C ALA A 331 . −42.063 3.476 9.384 1.00 16.93 . 1 2561 ATOM O O ALA A 331 . −41.998 4.151 8.371 1.00 19.05 . 1 2562 ATOM C CB ALA A 331 . −39.745 3.997 10.315 1.00 16.28 . 1 2563 ATOM N N GLY A 332 . −42.809 2.385 9.458 1.00 17.05 . 1 2564 ATOM C CA GLY A 332 . −43.666 2.031 8.340 1.00 19.13 . 1 2565 ATOM C C GLY A 332 . −43.078 1.181 7.227 1.00 18.83 . 1 2566 ATOM O O GLY A 332 . −43.544 1.223 6.093 1.00 19.90 . 1 2567 ATOM N N PHE A 333 . −42.004 0.480 7.523 1.00 16.79 . 1 2568 ATOM C CA PHE A 333 . −41.403 −0.427 6.569 1.00 15.57 . 1 2569 ATOM C C PHE A 333 . −42.078 −1.781 6.757 1.00 16.14 . 1 2570 ATOM O O PHE A 333 . −42.424 −2.162 7.898 1.00 17.31 . 1 2571 ATOM C CB PHE A 333 . −39.883 −0.505 6.780 1.00 15.38 . 1 2572 ATOM C CG PHE A 333 . −39.178 0.731 6.311 1.00 13.85 . 1 2573 ATOM C CD1 PHE A 333 . −39.157 1.857 7.111 1.00 12.94 . 1 2574 ATOM C CD2 PHE A 333 . −38.620 0.829 5.040 1.00 14.26 . 1 2575 ATOM C CE1 PHE A 333 . −38.608 3.030 6.652 1.00 12.85 . 1 2576 ATOM C CE2 PHE A 333 . −38.061 1.989 4.562 1.00 13.99 . 1 2577 ATOM C CZ PHE A 333 . −38.051 3.115 5.374 1.00 13.36 . 1 2578 ATOM N N GLN A 334 . −42.245 −2.512 5.655 1.00 15.09 . 1 2579 ATOM C CA GLN A 334 . −42.994 −3.781 5.717 1.00 14.72 . 1 2580 ATOM C C GLN A 334 . −42.201 −5.029 6.072 1.00 15.29 . 1 2581 ATOM O O GLN A 334 . −42.745 −5.946 6.674 1.00 16.46 . 1 2582 ATOM C CB GLN A 334 . −43.721 −4.052 4.410 1.00 14.80 . 1 2583 ATOM C CG GLN A 334 . −44.708 −2.969 4.020 1.00 16.13 . 1 2584 ATOM C CD GLN A 334 . −45.438 −3.346 2.746 1.00 17.84 . 1 2585 ATOM O OE1 GLN A 334 . −45.089 −2.876 1.652 1.00 23.79 . 1 2586 ATOM N NE2 GLN A 334 . −46.419 −4.219 2.867 1.00 12.74 . 1 2587 ATOM N N HIS A 335 . −40.950 −5.091 5.636 1.00 15.42 . 1 2588 ATOM C CA HIS A 335 . −40.095 −6.199 6.025 1.00 13.74 . 1 2589 ATOM C C HIS A 335 . −38.641 −5.795 5.870 1.00 14.56 . 1 2590 ATOM O O HIS A 335 . −38.352 −4.743 5.311 1.00 14.74 . 1 2591 ATOM C CB HIS A 335 . −40.406 −7.503 5.247 1.00 15.62 . 1 2592 ATOM C CG HIS A 335 . −40.147 −7.392 3.793 1.00 15.09 . 1 2593 ATOM N ND1 HIS A 335 . −39.114 −8.056 3.163 1.00 16.22 . 1 2594 ATOM C CD2 HIS A 335 . −40.772 −6.668 2.835 1.00 16.85 . 1 2595 ATOM C CE1 HIS A 335 . −39.112 −7.747 1.883 1.00 16.20 . 1 2596 ATOM N NE2 HIS A 335 . −40.116 −6.911 1.664 1.00 17.27 . 1 2597 ATOM N N TYR A 336 . −37.749 −6.584 6.445 1.00 14.21 . 1 2598 ATOM C CA TYR A 336 . −36.316 −6.310 6.414 1.00 14.88 . 1 2599 ATOM C C TYR A 336 . −35.501 −7.593 6.298 1.00 13.52 . 1 2600 ATOM O O TYR A 336 . −35.988 −8.681 6.592 1.00 15.86 . 1 2601 ATOM C CB TYR A 336 . −35.894 −5.546 7.695 1.00 15.69 . 1 2602 ATOM C CG TYR A 336 . −35.958 −6.412 8.958 1.00 14.91 . 1 2603 ATOM C CD1 TYR A 336 . −34.846 −7.152 9.387 1.00 16.16 . 1 2604 ATOM C CD2 TYR A 336 . −37.139 −6.532 9.676 1.00 16.30 . 1 2605 ATOM C CE1 TYR A 336 . −34.911 −7.991 10.492 1.00 17.21 . 1 2606 ATOM C CE2 TYR A 336 . −37.202 −7.374 10.807 1.00 17.24 . 1 2607 ATOM C CZ TYR A 336 . −36.107 −8.085 11.194 1.00 18.02 . 1 2608 ATOM O OH TYR A 336 . −36.202 −8.921 12.302 1.00 22.00 . 1 2609 ATOM N N LYS A 337 . −34.246 −7.446 5.934 1.00 14.19 . 1 2610 ATOM C CA LYS A 337 . −33.325 −8.557 5.806 1.00 15.41 . 1 2611 ATOM C C LYS A 337 . −31.975 −8.121 6.345 1.00 16.68 . 1 2612 ATOM O O LYS A 337 . −31.541 −7.000 6.079 1.00 17.92 . 1 2613 ATOM C CB LYS A 337 . −33.175 −8.925 4.357 1.00 15.86 . 1 2614 ATOM C CG LYS A 337 . −34.514 −9.421 3.838 1.00 15.83 . 1 2615 ATOM C CD LYS A 337 . −34.340 −9.819 2.415 1.00 18.41 . 1 2616 ATOM C CE LYS A 337 . −35.611 −10.516 1.886 1.00 16.11 . 1 2617 ATOM N NZ LYS A 337 . −35.439 −10.719 0.436 1.00 18.51 . 1 2618 ATOM N N ILE A 338 . −31.351 −8.973 7.142 1.00 15.62 . 1 2619 ATOM C CA ILE A 338 . −30.016 −8.690 7.700 1.00 15.68 . 1 2620 ATOM C C ILE A 338 . −29.022 −9.699 7.130 1.00 16.49 . 1 2621 ATOM O O ILE A 338 . −29.349 −10.884 7.047 1.00 18.41 . 1 2622 ATOM C CB ILE A 338 . −29.988 −8.787 9.254 1.00 14.73 . 1 2623 ATOM C CG1 ILE A 338 . −30.962 −7.751 9.843 1.00 15.64 . 1 2624 ATOM C CG2 ILE A 338 . −28.566 −8.558 9.790 1.00 15.52 . 1 2625 ATOM C CD1 ILE A 338 . −31.208 −7.849 11.346 1.00 17.25 . 1 2626 ATOM N N SER A 339 . −27.854 −9.237 6.694 1.00 15.31 . 1 2627 ATOM C CA SER A 339 . −26.784 −10.105 6.159 1.00 18.44 . 1 2628 ATOM C C SER A 339 . −25.472 −9.676 6.805 1.00 19.42 . 1 2629 ATOM O O SER A 339 . −25.289 −8.526 7.159 1.00 16.10 . 1 2630 ATOM C CB SER A 339 . −26.596 −9.877 4.638 1.00 20.09 . 1 2631 ATOM O OG SER A 339 . −27.783 −10.086 3.870 1.00 26.97 . 1 2632 ATOM N N PRO A 340 . −24.510 −10.589 6.959 1.00 19.22 . 1 2633 ATOM C CA PRO A 340 . −23.242 −10.152 7.554 1.00 18.85 . 1 2634 ATOM C C PRO A 340 . −22.508 −9.360 6.450 1.00 18.75 . 1 2635 ATOM O O PRO A 340 . −22.673 −9.631 5.260 1.00 19.95 . 1 2636 ATOM C CB PRO A 340 . −22.501 −11.467 7.844 1.00 21.67 . 1 2637 ATOM C CG PRO A 340 . −23.597 −12.494 7.860 1.00 22.65 . 1 2638 ATOM C CD PRO A 340 . −24.574 −12.053 6.835 1.00 21.16 . 1 2639 ATOM N N LEU A 341 . −21.737 −8.335 6.812 1.00 17.59 . 1 2640 ATOM C CA LEU A 341 . −21.021 −7.582 5.784 1.00 18.07 . 1 2641 ATOM C C LEU A 341 . −19.513 −7.730 5.948 1.00 19.09 . 1 2642 ATOM O O LEU A 341 . −18.845 −8.281 5.096 1.00 19.01 . 1 2643 ATOM C CB LEU A 341 . −21.414 −6.104 5.840 1.00 16.24 . 1 2644 ATOM C CG LEU A 341 . −20.788 −5.246 4.712 1.00 14.23 . 1 2645 ATOM C CD1 LEU A 341 . −21.331 −5.650 3.332 1.00 15.62 . 1 2646 ATOM C CD2 LEU A 341 . −21.071 −3.805 4.945 1.00 17.79 . 1 2647 ATOM N N THR A 342 . −18.962 −7.226 7.050 1.00 19.12 . 1 2648 ATOM C CA THR A 342 . −17.517 −7.388 7.273 1.00 20.65 . 1 2649 ATOM C C THR A 342 . −17.205 −7.034 8.705 1.00 19.41 . 1 2650 ATOM O O THR A 342 . −17.715 −6.050 9.240 1.00 16.57 . 1 2651 ATOM C CB THR A 342 . −16.654 −6.480 6.319 1.00 20.35 . 1 2652 ATOM O OG1 THR A 342 . −15.253 −6.576 6.681 1.00 22.61 . 1 2653 ATOM C CG2 THR A 342 . −17.079 −5.043 6.456 1.00 20.12 . 1 2654 ATOM N N GLY A 343 . −16.355 −7.856 9.347 1.00 19.34 . 1 2655 ATOM C CA GLY A 343 . −15.984 −7.607 10.739 1.00 19.08 . 1 2656 ATOM C C GLY A 343 . −17.183 −7.437 11.675 1.00 18.95 . 1 2657 ATOM O O GLY A 343 . −18.021 −8.317 11.805 1.00 19.77 . 1 2658 ATOM N N PHE A 344 . −17.227 −6.310 12.348 1.00 19.23 . 1 2659 ATOM C CA PHE A 344 . −18.304 −6.015 13.283 1.00 16.78 . 1 2660 ATOM C C PHE A 344 . −19.604 −5.558 12.624 1.00 15.60 . 1 2661 ATOM O O PHE A 344 . −20.594 −5.453 13.335 1.00 13.57 . 1 2662 ATOM C CB PHE A 344 . −17.868 −4.896 14.218 1.00 20.25 . 1 2663 ATOM C CG PHE A 344 . −16.785 −5.299 15.203 1.00 23.97 . 1 2664 ATOM C CD1 PHE A 344 . −15.460 −4.943 14.996 1.00 25.96 . 1 2665 ATOM C CD2 PHE A 344 . −17.114 −6.028 16.304 1.00 24.53 . 1 2666 ATOM C CE1 PHE A 344 . −14.467 −5.325 15.892 1.00 25.62 . 1 2667 ATOM C CE2 PHE A 344 . −16.129 −6.423 17.219 1.00 26.34 . 1 2668 ATOM C CZ PHE A 344 . −14.805 −6.062 16.994 1.00 25.89 . 1 2669 ATOM N N LEU A 345 . −19.610 −5.329 11.308 1.00 15.84 . 1 2670 ATOM C CA LEU A 345 . −20.808 −4.760 10.683 1.00 16.32 . 1 2671 ATOM C C LEU A 345 . −21.726 −5.660 9.909 1.00 15.30 . 1 2672 ATOM O O LEU A 345 . −21.288 −6.629 9.294 1.00 16.26 . 1 2673 ATOM C CB LEU A 345 . −20.369 −3.624 9.758 1.00 15.59 . 1 2674 ATOM C CG LEU A 345 . −19.559 −2.500 10.446 1.00 17.58 . 1 2675 ATOM C CD1 LEU A 345 . −19.020 −1.519 9.441 1.00 19.75 . 1 2676 ATOM C CD2 LEU A 345 . −20.403 −1.815 11.502 1.00 21.20 . 1 2677 ATOM N N SER A 346 . −23.013 −5.307 9.900 1.00 14.71 . 1 2678 ATOM C CA SER A 346 . −24.023 −6.016 9.081 1.00 13.38 . 1 2679 ATOM C C SER A 346 . −24.569 −5.123 8.003 1.00 14.90 . 1 2680 ATOM O O SER A 346 . −24.404 −3.914 8.056 1.00 15.37 . 1 2681 ATOM C CB SER A 346 . −25.191 −6.452 9.970 1.00 16.50 . 1 2682 ATOM O OG SER A 346 . −24.716 −7.330 10.996 1.00 18.63 . 1 2683 ATOM N N LEU A 347 . −25.258 −5.718 7.042 1.00 13.11 . 1 2684 ATOM C CA LEU A 347 . −25.888 −4.976 5.945 1.00 13.49 . 1 2685 ATOM C C LEU A 347 . −27.380 −5.259 6.192 1.00 13.70 . 1 2686 ATOM O O LEU A 347 . −27.802 −6.418 6.201 1.00 15.84 . 1 2687 ATOM C CB LEU A 347 . −25.453 −5.575 4.602 1.00 15.49 . 1 2688 ATOM C CG LEU A 347 . −25.864 −4.955 3.251 1.00 18.07 . 1 2689 ATOM C CD1 LEU A 347 . −27.328 −4.968 3.141 1.00 20.62 . 1 2690 ATOM C CD2 LEU A 347 . −25.334 −3.553 3.109 1.00 15.86 . 1 2691 ATOM N N ILE A 348 . −28.181 −4.220 6.372 1.00 11.99 . 1 2692 ATOM C CA ILE A 348 . −29.593 −4.418 6.630 1.00 12.84 . 1 2693 ATOM C C ILE A 348 . −30.361 −3.758 5.510 1.00 12.82 . 1 2694 ATOM O O ILE A 348 . −30.083 −2.616 5.156 1.00 14.09 . 1 2695 ATOM C CB ILE A 348 . −30.025 −3.736 7.975 1.00 11.96 . 1 2696 ATOM C CG1 ILE A 348 . −29.119 −4.180 9.120 1.00 14.14 . 1 2697 ATOM C CG2 ILE A 348 . −31.472 −4.030 8.301 1.00 15.23 . 1 2698 ATOM C CD1 ILE A 348 . −29.452 −3.453 10.485 1.00 15.07 . 1 2699 ATOM N N GLU A 349 . −31.347 −4.431 4.911 1.00 12.17 . 1 2700 ATOM C CA GLU A 349 . −32.139 −3.748 3.863 1.00 12.42 . 1 2701 ATOM C C GLU A 349 . −33.577 −3.709 4.337 1.00 13.50 . 1 2702 ATOM O O GLU A 349 . −34.078 −4.722 4.912 1.00 14.51 . 1 2703 ATOM C CB GLU A 349 . −32.020 −4.451 2.512 1.00 14.08 . 1 2704 ATOM C CG GLU A 349 . −30.592 −4.308 2.023 1.00 14.92 . 1 2705 ATOM C CD GLU A 349 . −30.395 −4.469 0.516 1.00 20.40 . 1 2706 ATOM O OE1 GLU A 349 . −30.371 −5.615 −0.006 1.00 23.82 . 1 2707 ATOM O OE2 GLU A 349 . −30.228 −3.434 −0.149 1.00 18.00 . 1 2708 ATOM N N ILE A 350 . −34.231 −2.548 4.172 1.00 12.45 . 1 2709 ATOM C CA ILE A 350 . −35.599 −2.407 4.629 1.00 11.76 . 1 2710 ATOM C C ILE A 350 . −36.470 −1.969 3.449 1.00 10.45 . 1 2711 ATOM O O ILE A 350 . −36.041 −1.192 2.580 1.00 11.73 . 1 2712 ATOM C CB ILE A 350 . −35.719 −1.478 5.887 1.00 13.16 . 1 2713 ATOM C CG1 ILE A 350 . −35.221 −0.092 5.556 1.00 15.00 . 1 2714 ATOM C CG2 ILE A 350 . −34.964 −2.103 7.094 1.00 15.43 . 1 2715 ATOM C CD1 ILE A 350 . −35.426 0.877 6.737 1.00 13.54 . 1 2716 ATOM N N TYR A 351 . −37.682 −2.520 3.405 1.00 11.14 . 1 2717 ATOM C CA TYR A 351 . −38.585 −2.325 2.232 1.00 11.12 . 1 2718 ATOM C C TYR A 351 . −39.894 −1.675 2.627 1.00 12.17 . 1 2719 ATOM O O TYR A 351 . −40.608 −2.167 3.468 1.00 14.80 . 1 2720 ATOM C CB TYR A 351 . −38.799 −3.739 1.584 1.00 13.24 . 1 2721 ATOM C CG TYR A 351 . −37.510 −4.465 1.288 1.00 14.67 . 1 2722 ATOM C CD1 TYR A 351 . −36.981 −5.314 2.253 1.00 17.18 . 1 2723 ATOM C CD2 TYR A 351 . −36.832 −4.279 0.104 1.00 17.56 . 1 2724 ATOM C CE1 TYR A 351 . −35.778 −5.986 2.074 1.00 18.49 . 1 2725 ATOM C CE2 TYR A 351 . −35.576 −4.953 −0.112 1.00 15.92 . 1 2726 ATOM C CZ TYR A 351 . −35.095 −5.799 0.921 1.00 16.83 . 1 2727 ATOM O OH TYR A 351 . −33.868 −6.417 0.791 1.00 22.04 . 1 2728 ATOM N N PRO A 352 . −40.181 −0.498 2.053 1.00 12.73 . 1 2729 ATOM C CA PRO A 352 . −41.397 0.253 2.352 1.00 16.30 . 1 2730 ATOM C C PRO A 352 . −42.725 −0.329 1.995 1.00 20.70 . 1 2731 ATOM O O PRO A 352 . −43.638 0.009 2.790 1.00 24.71 . 1 2732 ATOM C CB PRO A 352 . −41.125 1.634 1.697 1.00 16.17 . 1 2733 ATOM C CG PRO A 352 . −40.260 1.308 0.587 1.00 18.91 . 1 2734 ATOM C CD PRO A 352 . −39.290 0.290 1.180 1.00 15.00 . 1 2735 #352 . TER # . . PRO A 352 . . . . . . . 1 2736 HETA N N SAH . 1699 . −21.510 7.575 5.867 1.00 11.21 . 2 2737 HETA C CA SAH . 1699 . −20.240 8.294 6.361 1.00 13.10 . 2 2738 HETA C CB SAH . 1699 . −20.533 8.912 7.646 1.00 17.90 . 2 2739 HETA C CG SAH . 1699 . −19.641 9.713 8.501 1.00 20.01 . 2 2740 HETA S SD SAH . 1699 . −20.417 10.156 10.070 1.00 17.57 . 2 2741 HETA C C SAH . 1699 . −19.182 7.313 6.515 1.00 14.54 . 2 2742 HETA O O SAH . 1699 . −18.010 7.788 6.616 1.00 14.80 . 2 2743 HETA O OXT SAH . 1699 . −19.518 6.093 6.608 1.00 14.12 . 2 2744 HETA C C5* SAH . 1699 . −22.083 10.855 9.271 1.00 22.32 . 2 2745 HETA C C4* SAH . 1699 . −22.226 11.744 9.216 1.00 19.04 . 2 2746 HETA O O4* SAH . 1699 . −23.686 12.159 9.204 1.00 12.43 . 2 2747 HETA C C3* SAH . 1699 . −21.410 13.045 9.036 1.00 15.02 . 2 2748 HETA O O3* SAH . 1699 . −20.863 13.101 7.685 1.00 15.20 . 2 2749 HETA C C2* SAH . 1699 . −22.456 14.091 9.278 1.00 12.56 . 2 2750 HETA O O2* SAH . 1699 . −22.145 15.335 8.683 1.00 14.30 . 2 2751 HETA C C1* SAH . 1699 . −23.822 13.605 9.129 1.00 15.58 . 2 2752 HETA N N9 SAH . 1699 . −24.962 14.285 9.288 1.00 12.49 . 2 2753 HETA C C8 SAH . 1699 . −25.245 14.673 10.603 1.00 14.46 . 2 2754 HETA N N7 SAH . 1699 . −26.337 15.301 10.701 1.00 12.73 . 2 2755 HETA C C5 SAH . 1699 . −26.835 15.356 9.428 1.00 12.30 . 2 2756 HETA C C6 SAH . 1699 . −28.095 15.975 8.915 1.00 11.06 . 2 2757 HETA N N6 SAH . 1699 . −28.958 16.606 9.681 1.00 12.89 . 2 2758 HETA N N1 SAH . 1699 . −28.271 15.834 7.584 1.00 13.17 . 2 2759 HETA C C2 SAH . 1699 . −27.378 15.190 6.762 1.00 12.01 . 2 2760 HETA N N3 SAH . 1699 . −26.216 14.621 7.176 1.00 11.32 . 2 2761 HETA C C4 SAH . 1699 . −26.003 14.734 8.508 1.00 12.41 . 2 2762 HETA C C1 HMO . 2000 . −19.285 6.924 14.489 1.00 23.88 . 3 2763 HETA C C2 HMO . 2000 . −18.664 5.823 15.163 1.00 24.10 . 3 2764 HETA C C3 HMO . 2000 . −17.909 5.973 16.384 1.00 25.72 . 3 2765 HETA C C4 HMO . 2000 . −17.789 7.301 16.929 1.00 23.75 . 3 2766 HETA C C5 HMO . 2000 . −18.415 8.473 16.305 1.00 24.37 . 3 2767 HETA C C6 HMO . 2000 . −19.155 8.273 15.100 1.00 23.20 . 3 2768 HETA C C7 HMO . 2000 . −16.983 7.486 18.154 1.00 24.74 . 3 2769 HETA C C8 HMO . 2000 . −16.876 8.916 18.650 1.00 23.90 . 3 2770 HETA C C9 HMO . 2000 . −17.539 9.942 17.964 1.00 23.50 . 3 2771 HETA O O10 HMO . 2000 . −18.323 9.742 16.789 1.00 23.69 . 3 2772 HETA C C11 HMO . 2000 . −16.045 9.180 19.829 1.00 23.87 . 3 2773 HETA C C12 HMO . 2000 . −16.285 8.519 21.099 1.00 23.35 . 3 2774 HETA C C13 HMO . 2000 . −15.472 8.778 22.213 1.00 21.62 . 3 2775 HETA C C14 HMO . 2000 . −14.321 9.773 22.063 1.00 20.75 . 3 2776 HETA C C15 HMO . 2000 . −14.085 10.420 20.830 1.00 23.59 . 3 2777 HETA C C16 HMO . 2000 . −14.895 10.163 19.720 1.00 23.26 . 3 2778 HETA O O17 HMO . 2000 . −13.568 10.048 23.027 1.00 23.73 . 3 2779 HETA O O18 HMO . 2000 . −16.419 6.466 18.701 1.00 23.98 . 3 2780 HETA O O19 HMO . 2000 . −19.966 6.719 13.273 1.00 22.20 . 3 2781 HETA C C20 HMO . 2000 . −20.522 7.742 12.575 1.00 21.18 . 3 2782 HETA O O HOH . 1 . −20.792 6.726 3.294 1.00 12.43 . 4 2783 HETA O O HOH . 2 . −24.221 6.996 4.812 1.00 11.94 . 4 2784 HETA O O HOH . 3 . −32.408 18.925 2.789 1.00 13.25 . 4 2785 HETA O O HOH . 4 . −20.308 8.686 −0.017 1.00 12.46 . 4 2786 HETA O O HOH . 5 . −26.646 3.614 9.570 1.00 11.73 . 4 2787 HETA O O HOH . 6 . −18.305 7.903 2.717 1.00 13.50 . 4 2788 HETA O O HOH . 7 . −22.551 0.501 14.122 1.00 12.99 . 4 2789 HETA O O HOH . 8 . −16.754 5.661 3.547 1.00 16.09 . 4 2790 HETA O O HOH . 9 . 1.335 10.450 24.844 1.00 14.39 . 4 2791 HETA O O HOH . 10 . −26.093 −0.689 15.714 1.00 13.16 . 4 2792 HETA O O HOH . 11 . −20.805 14.989 36.077 1.00 16.81 . 4 2793 HETA O O HOH . 12 . −28.688 −2.926 22.226 1.00 15.89 . 4 2794 HETA O O HOH . 13 . −35.886 −12.089 −2.217 1.00 13.47 . 4 2795 HETA O O HOH . 14 . −15.620 7.003 5.751 1.00 16.14 . 4 2796 HETA O O HOH . 15 . 13.232 1.139 6.255 1.00 17.38 . 4 2797 HETA O O HOH . 16 . −27.930 1.388 15.989 1.00 15.36 . 4 2798 HETA O O HOH . 17 . −29.294 23.269 1.765 1.00 17.96 . 4 2799 HETA O O HOH . 18 . −25.724 12.201 −9.508 1.00 18.00 . 4 2800 HETA O O HOH . 19 . −17.728 9.220 34.859 1.00 13.51 . 4 2801 HETA O O HOH . 20 . 0.132 13.840 23.977 1.00 17.78 . 4 2802 HETA O O HOH . 21 . −15.611 3.916 7.378 1.00 17.49 . 4 2803 HETA O O HOH . 22 . −23.097 −6.755 13.165 1.00 14.53 . 4 2804 HETA O O HOH . 23 . −30.321 11.614 19.019 1.00 14.68 . 4 2805 HETA O O HOH . 24 . −37.885 −10.201 5.091 1.00 15.63 . 4 2806 HETA O O HOH . 25 . 13.513 5.726 33.570 1.00 19.62 . 4 2807 HETA O O HOH . 26 . −25.220 10.952 11.531 1.00 17.75 . 4 2808 HETA O O HOH . 27 . −31.020 18.178 28.437 1.00 20.66 . 4 2809 HETA O O HOH . 28 . −29.335 −7.902 3.862 1.00 20.12 . 4 2810 HETA O O HOH . 29 . 5.799 −2.997 32.619 1.00 18.19 . 4 2811 HETA O O HOH . 30 . −5.087 11.647 20.764 1.00 17.58 . 4 2812 HETA O O HOH . 31 . −27.370 17.286 12.391 1.00 20.39 . 4 2813 HETA O O HOH . 32 . −39.709 10.479 16.051 1.00 20.08 . 4 2814 HETA O O HOH . 33 . −16.777 10.241 3.369 1.00 15.38 . 4 2815 HETA O O HOH . 36 . −27.957 20.376 7.629 1.00 18.82 . 4 2816 HETA O O HOH . 37 . 11.487 7.979 36.151 1.00 20.53 . 4 2817 HETA O O HOH . 38 . −23.306 −9.454 19.595 1.00 19.74 . 4 2818 HETA O O HOH . 39 . 13.341 2.306 12.113 1.00 18.19 . 4 2819 HETA O O HOH . 40 . −27.583 12.347 18.283 1.00 16.89 . 4 2820 HETA O O HOH . 42 . −19.719 16.448 9.873 1.00 19.66 . 4 2821 HETA O O HOH . 43 . −21.572 5.795 −11.806 1.00 20.52 . 4 2822 HETA O O HOH . 44 . 0.966 4.290 14.658 1.00 17.18 . 4 2823 HETA O O HOH . 45 . −33.303 13.545 −6.524 1.00 20.27 . 4 2824 HETA O O HOH . 46 . −24.029 −1.828 25.928 1.00 18.51 . 4 2825 HETA O O HOH . 47 . −24.321 16.037 19.853 1.00 19.54 . 4 2826 HETA O O HOH . 48 . 7.155 4.220 32.608 1.00 18.36 . 4 2827 HETA O O HOH . 49 . −34.336 12.033 21.048 1.00 20.78 . 4 2828 HETA O O HOH . 50 . −17.108 10.235 6.150 1.00 20.72 . 4 2829 HETA O O HOH . 51 . 3.794 4.294 14.477 1.00 19.48 . 4 2830 HETA O O HOH . 52 . −19.253 −8.492 0.371 1.00 21.58 . 4 2831 HETA O O HOH . 53 . −39.177 −8.689 8.262 1.00 23.37 . 4 2832 HETA O O HOH . 54 . −12.744 14.665 16.202 1.00 20.91 . 4 2833 HETA O O HOH . 55 . 17.622 −3.606 16.844 1.00 19.86 . 4 2834 HETA O O HOH . 56 . −32.010 10.371 −8.042 1.00 25.67 . 4 2835 HETA O O HOH . 57 . −18.211 12.707 7.397 1.00 23.59 . 4 2836 HETA O O HOH . 58 . −26.559 6.679 24.507 1.00 18.34 . 4 2837 HETA O O HOH . 59 . −21.858 18.012 −7.659 1.00 22.35 . 4 2838 HETA O O HOH . 60 . −29.973 6.128 22.853 1.00 21.18 . 4 2839 HETA O O HOH . 61 . −40.508 −2.624 −5.172 1.00 20.62 . 4 2840 HETA O O HOH . 63 . 0.615 4.904 11.263 1.00 19.89 . 4 2841 HETA O O HOH . 64 . −33.553 0.826 19.763 1.00 22.91 . 4 2842 HETA O O HOH . 65 . −32.653 5.804 22.147 1.00 18.49 . 4 2843 HETA O O HOH . 66 . 10.867 −2.403 6.471 1.00 22.61 . 4 2844 HETA O O HOH . 68 . −23.343 22.894 7.352 1.00 24.07 . 4 2845 HETA O O HOH . 69 . −7.667 10.785 13.246 1.00 19.62 . 4 2846 HETA O O HOH . 70 . −2.804 −0.804 26.008 1.00 20.49 . 4 2847 HETA O O HOH . 71 . 8.898 9.192 16.915 1.00 24.39 . 4 2848 HETA O O HOH . 72 . −30.167 13.121 21.432 1.00 19.77 . 4 2849 HETA O O HOH . 73 . −12.977 3.640 0.968 1.00 20.89 . 4 2850 HETA O O HOH . 74 . −40.181 11.991 −2.062 1.00 24.61 . 4 2851 HETA O O HOH . 75 . −35.912 7.998 21.791 1.00 22.74 . 4 2852 HETA O O HOH . 76 . −39.258 12.845 9.748 1.00 19.06 . 4 2853 HETA O O HOH . 77 . 16.381 5.499 32.683 1.00 21.88 . 4 2854 HETA O O HOH . 78 . −29.953 −9.763 17.606 1.00 22.01 . 4 2855 HETA O O HOH . 79 . −28.774 −9.959 21.468 1.00 25.25 . 4 2856 HETA O O HOH . 80 . −23.092 0.369 −13.905 1.00 22.40 . 4 2857 HETA O O HOH . 81 . −36.068 −0.066 19.062 1.00 22.32 . 4 2858 HETA O O HOH . 82 . −13.416 −6.266 −4.084 1.00 28.67 . 4 2859 HETA O O HOH . 83 . −27.596 17.475 34.450 1.00 24.51 . 4 2860 HETA O O HOH . 84 . −15.773 18.375 3.939 1.00 25.31 . 4 2861 HETA O O HOH . 85 . −20.036 −5.727 28.579 1.00 24.67 . 4 2862 HETA O O HOH . 86 . −37.586 4.762 −5.467 1.00 20.26 . 4 2863 HETA O O HOH . 87 . −22.340 −13.650 22.122 1.00 24.11 . 4 2864 HETA O O HOH . 88 . −2.808 11.874 19.152 1.00 21.30 . 4 2865 HETA O O HOH . 89 . −13.777 −5.914 2.029 1.00 24.14 . 4 2866 HETA O O HOH . 90 . −13.194 6.230 −2.127 1.00 24.19 . 4 2867 HETA O O HOH . 91 . −22.266 −9.574 28.533 1.00 26.55 . 4 2868 HETA O O HOH . 92 . −40.742 7.029 11.042 1.00 25.34 . 4 2869 HETA O O HOH . 93 . −41.824 −5.629 −0.360 1.00 27.02 . 4 2870 HETA O O HOH . 94 . 20.543 3.768 23.243 1.00 26.77 . 4 2871 HETA O O HOH . 95 . 19.002 −2.838 24.316 1.00 26.72 . 4 2872 HETA O O HOH . 96 . −24.862 19.382 15.862 1.00 29.74 . 4 2873 HETA O O HOH . 97 . 8.459 −6.927 13.832 1.00 26.20 . 4 2874 HETA O O HOH . 98 . −30.898 −7.829 1.519 1.00 25.12 . 4 2875 HETA O O HOH . 99 . −14.358 22.535 10.212 1.00 27.28 . 4 2876 HETA O O HOH . 100 . −42.461 8.797 5.310 1.00 24.52 . 4 2877 HETA O O HOH . 101 . −32.958 18.013 31.823 1.00 27.20 . 4 2878 HETA O O HOH . 102 . −6.817 2.008 6.535 1.00 21.54 . 4 2879 HETA O O HOH . 103 . −39.621 −1.966 −1.546 1.00 26.69 . 4 2880 HETA O O HOH . 104 . −15.902 17.452 6.305 1.00 26.96 . 4 2881 HETA O O HOH . 106 . 4.628 −11.264 16.922 1.00 25.69 . 4 2882 HETA O O HOH . 107 . −28.539 5.321 −14.135 1.00 25.02 . 4 2883 HETA O O HOH . 108 . −9.733 23.272 15.292 1.00 27.25 . 4 2884 HETA O O HOH . 109 . −44.698 11.816 −5.848 1.00 33.95 . 4 2885 HETA O O HOH . 110 . 0.347 −11.391 16.280 1.00 29.85 . 4 2886 HETA O O HOH . 111 . −10.004 −0.077 5.196 1.00 27.67 . 4 2887 HETA O O HOH . 112 . −37.841 15.207 10.882 1.00 23.24 . 4 2888 HETA O O HOH . 113 . −10.551 14.042 17.844 1.00 25.27 . 4 2889 HETA O O HOH . 114 . −40.495 14.030 −8.452 1.00 23.35 . 4 2890 HETA O O HOH . 115 . −6.092 12.856 14.864 1.00 29.04 . 4 2891 HETA O O HOH . 116 . 21.103 −2.999 19.668 1.00 28.12 . 4 2892 HETA O O HOH . 118 . 5.695 −7.864 29.127 1.00 25.73 . 4 2893 HETA O O HOH . 119 . −13.449 11.251 −0.129 1.00 28.98 . 4 2894 HETA O O HOH . 120 . −8.259 −3.353 28.284 1.00 28.38 . 4 2895 HETA O O HOH . 121 . −31.392 −5.094 −6.007 1.00 27.17 . 4 2896 HETA O O HOH . 124 . −8.884 14.529 29.351 1.00 27.77 . 4 2897 HETA O O HOH . 125 . −38.628 8.118 −4.956 1.00 24.08 . 4 2898 HETA O O HOH . 126 . −24.617 −10.005 14.352 1.00 31.16 . 4 2899 HETA O O HOH . 127 . −17.202 16.149 8.910 1.00 28.04 . 4 2900 HETA O O HOH . 128 . −32.920 15.672 35.754 1.00 29.33 . 4 2901 HETA O O HOH . 129 . −39.467 16.434 2.865 1.00 26.18 . 4 2902 HETA O O HOH . 130 . −19.998 −9.099 13.680 1.00 30.80 . 4 2903 HETA O O HOH . 131 . −5.162 −4.649 30.458 1.00 29.27 . 4 2904 HETA O O HOH . 132 . 18.955 12.223 31.295 1.00 28.19 . 4 2905 HETA O O HOH . 133 . −35.735 −10.827 8.201 1.00 28.11 . 4 2906 HETA O O HOH . 134 . −34.119 −11.774 10.188 1.00 32.27 . 4 2907 HETA O O HOH . 135 . −19.854 7.556 −12.481 1.00 30.66 . 4 2908 HETA O O HOH . 136 . 10.834 −8.809 29.575 1.00 26.65 . 4 2909 HETA O O HOH . 137 . −35.972 16.563 14.015 1.00 30.01 . 4 2910 HETA O O HOH . 138 . −14.628 −10.035 8.352 1.00 29.64 . 4 2911 HETA O O HOH . 139 . −3.027 14.919 23.900 1.00 26.44 . 4 2912 HETA O O HOH . 140 . −0.113 −5.116 30.432 1.00 22.12 . 4 2913 HETA O O HOH . 141 . −34.228 19.856 11.010 1.00 31.61 . 4 2914 HETA O O HOH . 142 . −47.567 1.118 −1.738 1.00 32.25 . 4 2915 HETA O O HOH . 143 . 13.880 9.435 35.826 1.00 22.80 . 4 2916 HETA O O HOH . 144 . 5.793 −10.532 24.812 1.00 37.63 . 4 2917 HETA O O HOH . 145 . 12.474 −7.415 6.782 1.00 31.22 . 4 2918 HETA O O HOH . 146 . −33.061 22.332 7.843 1.00 28.37 . 4 2919 HETA O O HOH . 147 . −14.624 −7.309 −0.225 1.00 30.13 . 4 2920 HETA O O HOH . 148 . −17.771 9.174 −11.002 1.00 27.27 . 4 2921 HETA O O HOH . 149 . −6.176 17.436 13.145 1.00 29.80 . 4 2922 HETA O O HOH . 150 . −17.313 20.157 8.895 1.00 30.89 . 4 2923 HETA O O HOH . 151 . −26.017 20.173 −5.509 1.00 25.98 . 4 2924 HETA O O HOH . 152 . −27.451 2.103 −13.113 1.00 26.09 . 4 2925 HETA O O HOH . 153 . −14.614 4.634 10.778 1.00 24.66 . 4 2926 HETA O O HOH . 154 . 9.558 8.693 14.110 1.00 28.27 . 4 2927 HETA O O HOH . 155 . −33.388 −2.836 −7.780 1.00 35.32 . 4 2928 HETA O O HOH . 156 . −7.475 7.368 7.617 1.00 27.37 . 4 2929 HETA O O HOH . 157 . −38.830 19.988 3.558 1.00 31.15 . 4 2930 HETA O O HOH . 158 . −33.499 6.661 −10.828 1.00 32.93 . 4 2931 HETA O O HOH . 159 . −15.211 −7.023 −7.013 1.00 31.81 . 4 2932 HETA O O HOH . 160 . −35.383 0.788 −6.230 1.00 27.00 . 4 2933 HETA O O HOH . 161 . −13.445 16.830 28.366 1.00 31.35 . 4 2934 HETA O O HOH . 162 . −28.946 −7.639 23.152 1.00 30.59 . 4 2935 HETA O O HOH . 163 . 2.478 9.580 15.332 1.00 34.05 . 4 2936 HETA O O HOH . 164 . −1.935 7.971 13.165 1.00 25.55 . 4 2937 HETA O O HOH . 165 . −20.365 −6.238 −7.482 1.00 24.91 . 4 2938 HETA O O HOH . 166 . −41.607 −2.670 −0.421 1.00 24.69 . 4 2939 HETA O O HOH . 167 . −6.057 13.451 11.805 1.00 30.48 . 4 2940 HETA O O HOH . 168 . −31.715 15.572 18.176 1.00 32.11 . 4 2941 HETA O O HOH . 169 . −20.696 20.653 −3.662 1.00 37.44 . 4 2942 HETA O O HOH . 170 . 16.115 −8.267 15.855 1.00 32.54 . 4 2943 HETA O O HOH . 171 . −38.473 −10.683 12.284 1.00 36.44 . 4 2944 HETA O O HOH . 173 . −40.070 18.350 6.732 1.00 31.08 . 4 2945 HETA O O HOH . 174 . −12.795 −9.516 58.295 1.00 40.73 . 4 2946 HETA O O HOH . 175 . −33.406 −3.328 −4.714 1.00 30.20 . 4 2947 HETA O O HOH . 176 . 20.333 12.235 28.232 1.00 32.92 . 4 2948 HETA O O HOH . 177 . −23.759 22.314 27.154 1.00 37.34 . 4 2949 HETA O O HOH . 178 . −2.630 −6.405 11.081 1.00 27.09 . 4 2950 HETA O O HOH . 180 . −1.298 −9.918 19.950 1.00 33.07 . 4 2951 HETA O O HOH . 181 . −11.539 20.174 8.358 1.00 30.05 . 4 2952 HETA O O HOH . 182 . −27.296 11.373 42.192 1.00 35.62 . 4 2953 HETA O O HOH . 183 . −45.108 4.674 −3.739 1.00 31.13 . 4 2954 HETA O O HOH . 184 . −34.374 −8.720 −0.744 1.00 30.25 . 4 2955 HETA O O HOH . 185 . −25.284 −5.542 −9.082 1.00 27.21 . 4 2956 HETA O O HOH . 186 . −19.685 6.384 −16.341 1.00 34.04 . 4 2957 HETA O O HOH . 187 . −27.759 15.579 −7.869 1.00 28.21 . 4 2958 HETA O O HOH . 188 . −18.841 −13.750 15.826 1.00 32.31 . 4 2959 HETA O O HOH . 189 . −4.625 10.664 13.024 1.00 28.33 . 4 2960 HETA O O HOH . 190 . −12.389 10.194 30.442 1.00 31.12 . 4 2961 HETA O O HOH . 191 . −29.411 −12.402 9.999 1.00 32.48 . 4 2962 HETA O O HOH . 192 . −13.106 −10.427 16.618 1.00 29.89 . 4 2963 HETA O O HOH . 195 . 0.855 11.477 16.361 1.00 29.19 . 4 2964 HETA O O HOH . 196 . −42.588 11.112 −1.785 1.00 29.45 . 4 2965 HETA O O HOH . 197 . 12.610 −14.642 23.500 1.00 36.03 . 4 2966 HETA O O HOH . 200 . −32.819 −11.577 −0.270 1.00 30.82 . 4 2967 HETA O O HOH . 201 . −12.100 6.091 −4.939 1.00 30.72 . 4 2968 HETA O O HOH . 202 . −8.183 18.395 23.760 1.00 32.26 . 4 2969 HETA O O HOH . 203 . −44.542 −1.238 9.322 1.00 38.38 . 4 2970 HETA O O HOH . 204 . −30.196 −11.345 15.431 1.00 36.41 . 4 2971 HETA O O HOH . 205 . 16.536 −9.594 21.134 1.00 31.93 . 4 2972 HETA O O HOH . 207 . −17.145 5.604 −12.682 1.00 29.15 . 4 2973 HETA O O HOH . 209 . −45.413 −5.636 7.569 1.00 31.86 . 4 2974 HETA O O HOH . 210 . −24.404 4.958 25.802 1.00 31.12 . 4 2975 HETA O O HOH . 214 . −5.856 4.880 7.904 1.00 24.33 . 4 2976 HETA O O HOH . 1001 . 0.420 6.651 13.268 1.00 19.75 . 4 2977 HETA O O HOH . 1002 . −22.647 −5.160 29.087 1.00 20.57 . 4 2978 HETA O O HOH . 1003 . −43.184 −2.982 −4.317 1.00 20.34 . 4 2979 HETA O O HOH . 1004 . −32.563 13.451 22.664 1.00 22.10 . 4 2980 HETA O O HOH . 1005 . 12.748 3.602 35.070 1.00 22.62 . 4 2981 HETA O O HOH . 1006 . −40.913 10.441 13.544 1.00 23.65 . 4 2982 HETA O O HOH . 1007 . −28.272 −0.977 24.054 1.00 22.27 . 4 2983 HETA O O HOH . 1008 . −28.679 22.748 6.663 1.00 22.05 . 4 2984 HETA O O HOH . 1009 . −16.601 9.673 −15.389 1.00 27.17 . 4 2985 HETA O O HOH . 1010 . −19.996 0.678 14.999 1.00 23.94 . 4 2986 HETA O O HOH . 1011 . −37.591 2.628 −7.305 1.00 28.64 . 4 2987 HETA O O HOH . 1012 . −36.482 −1.266 21.720 1.00 25.09 . 4 2988 HETA O O HOH . 1013 . 12.809 5.041 12.309 1.00 22.25 . 4 2989 HETA O O HOH . 1014 . −25.528 −3.578 −11.137 1.00 28.84 . 4 2990 HETA O O HOH . 1015 . −22.300 16.034 38.181 1.00 24.02 . 4 2991 HETA O O HOH . 1016 . 8.271 −8.017 30.362 1.00 26.37 . 4 2992 HETA O O HOH . 1017 . 11.049 0.452 5.053 1.00 26.79 . 4 2993 HETA O O HOH . 1018 . −25.619 0.439 −12.632 1.00 27.56 . 4 2994 HETA O O HOH . 1019 . −42.730 8.369 12.813 1.00 28.74 . 4 2995 HETA O O HOH . 1020 . −22.277 −1.848 −15.459 1.00 28.27 . 4 2996 HETA O O HOH . 1021 . −39.187 −4.168 −3.405 1.00 25.46 . 4 2997 HETA O O HOH . 1022 . −28.699 20.255 10.259 1.00 30.72 . 4 2998 HETA O O HOH . 1023 . −30.728 −0.514 24.286 1.00 26.62 . 4 2999 HETA O O HOH . 1024 . −15.420 17.206 30.101 1.00 26.18 . 4 3000 HETA O O HOH . 1025 . −23.735 −7.568 29.334 1.00 25.90 . 4 3001 HETA O O HOH . 1026 . −41.064 12.518 11.921 1.00 24.19 . 4 3002 HETA O O HOH . 1027 . −6.041 −6.685 50.482 1.00 23.31 . 4 3003 HETA O O HOH . 1028 . −28.744 15.103 19.358 1.00 27.21 . 4 3004 HETA O O HOH . 1029 . −38.129 6.817 22.129 1.00 30.86 . 4 3005 HETA O O HOH . 1030 . −16.239 −5.208 −8.864 1.00 25.10 . 4 3006 HETA O O HOH . 1032 . −11.427 4.943 −0.825 1.00 25.48 . 4 3007 HETA O O HOH . 1033 . −6.181 −2.233 34.049 1.00 27.13 . 4 3008 HETA O O HOH . 1034 . −14.328 10.113 6.156 1.00 29.03 . 4 3009 HETA O O HOH . 1035 . −10.329 8.520 31.469 1.00 28.81 . 4 3010 HETA O O HOH . 1037 . −25.774 21.723 8.943 1.00 25.58 . 4 3011 HETA O O HOH . 1038 . −35.268 14.216 19.258 1.00 31.03 . 4 3012 HETA O O HOH . 1039 . −12.030 8.706 −1.472 1.00 29.60 . 4 3013 HETA O O HOH . 1040 . 7.981 −4.264 33.523 1.00 29.42 . 4 3014 HETA O O HOH . 1042 . 14.102 12.113 36.036 1.00 29.16 . 4 3015 HETA O O HOH . 1046 . −31.886 15.055 −8.057 1.00 28.39 . 4 3016 HETA O O HOH . 1049 . −2.020 4.512 6.125 1.00 31.58 . 4 3017 HETA O O HOH . 1050 . −25.230 −9.877 10.500 1.00 27.98 . 4 3018 HETA O O HOH . 1052 . −41.464 9.459 17.906 1.00 35.56 . 4 3019 HETA O O HOH . 1053 . −29.858 16.532 −6.938 1.00 30.16 . 4 3020 HETA O O HOH . 1054 . −27.031 17.551 37.190 1.00 30.35 . 4 3021 HETA O O HOH . 1055 . −24.069 −8.928 2.918 1.00 30.55 . 4 3022 HETA O O HOH . 1066 . −13.183 −11.876 45.674 1.00 32.82 . 4 3023 HETA O O HOH . 1067 . −37.357 8.751 −7.389 1.00 29.77 . 4 3024 HETA O O HOH . 1068 . −3.552 14.464 18.203 1.00 32.75 . 4 3025 HETA O O HOH . 1071 . −29.402 16.731 22.154 1.00 31.16 . 4 3026 HETA O O HOH . 1074 . −15.543 9.147 −12.834 1.00 30.41 . 4 3027 HETA O O HOH . 1080 . −37.937 1.836 19.502 1.00 32.27 . 4 3028 HETA O O HOH . 1094 . −28.168 −5.055 23.739 1.00 30.89 . 4 3029 

1. A method of predicting the activity and/or substrate specificity of a putative O-methyltransferase, said method comprising: comparing a three-dimensional representation of a known O-methyltransferase and the three-dimensional representation of said putative O-methyltransferase, wherein similarities and/or differences between the two representations are predictive of O-methyltransferase activity and/or substrate specificity.
 2. The method of claim 1, wherein the known O-methyltransferase is Chalcone O-methyltransferase (ChOMT) or isoflavone O-methyltransferase (IOMT).
 3. The method of claim 2, wherein the known O-methyltransferase has structural coordinates as set forth in Appendix A, Appendix B, Appendix C, Appendix D, PDB Accession No: 1FPQ, PDB Accession No: 1FPX, PDB Accession No: 1FP 1, or PDB Accession No: 1FP2.
 4. The method of claim 1, wherein the putative O-methyltransferase is a mutant of a known O-methyltransferase.
 5. A crystalline form of an O-methyltransferase having a set of structural coordinates as set forth in Appendix A, Appendix B, Appendix C, Appendix D, PDB Accession No: 1FPQ, PDB Accession No: 1FPX, PDB Accession No: 1FP1, or PDB Accession No: 1FP2.
 6. The crystalline O-methyltransferase of claim 5, wherein the O-methyltransferase is a Chalcone O-methyltransferase (ChOMT) or isoflavone O-methyltransferase(IOMT).
 7. A crystalline complex comprising an O-methyltransferase and an O-methyltransferase substrate.
 8. The crystalline complex of claim 7, wherein the O-methyltransferase is Chalcone O-methyltransferase (ChOMT) or isoflavone O-methyltransferase (IOMT).
 9. The crystalline complex of claim 7, wherein the O-methyltransferase is a non-native O-methyltransferase.
 10. The crystalline complex of claim 7, wherein the O-methyltransferase substrate is S-adenosyl-L-methionine (SAM).
 11. The crystalline complex of claim 7, wherein the complex has atomic coordinates as set forth in Appendix A, Appendix B, Appendix C, Appendix D, PDB Accession No: 1FPQ, PDB Accession No: 1FPX, PDB Accession No: 1FP1, or PDB Accession No: 1FP2.
 12. A method of identifying a potential substrate of an isoflavone O-methyltransferase, said method comprising: (a) defining an active site of said isoflavone O-methyltransferase based on a plurality of atomic coordinates of said isoflavone O-methyltransferase; (b) identifying a potential substrate that fits the active site of (a); and (c) contacting the isoflavone O-methyltransferase with the potential substrate and determining its activity thereon.
 13. (canceled)
 14. The method of claim 12, wherein the isoflavone O-methyltransferase is a mutant of a known isoflavone O-methyltransferase.
 15. (canceled)
 16. The method of claim 12, wherein the plurality of atomic coordinates are as set forth in Appendix B or Appendix D, or portions thereof.
 17. A method of identifying a potential inhibitor of an isoflavone O-methyltransferase, said method comprising: (a) contacting a potential compound that fits an active site based on a plurality of atomic coordinates of said isoflavone O-methyltransferase; and (b) determining the ability of said compound to inhibit the activity of said isoflavone O-methyltransferase.
 18. (canceled)
 19. The method of claim 17, wherein the isoflavone O-methyltransferase is a mutant of a known isoflavone O-methyltransferase.
 20. (canceled)
 21. The method of claim 17, wherein the plurality of atomic coordinates are as set forth in Appendix B or Appendix D, or portions thereof. 22.-23. (canceled) 